alanine and heme

alanine has been researched along with heme in 85 studies

Research

Studies (85)

Timeframe	Studies, this research(%)	All Research%
pre-1990	10 (11.76)	18.7374
1990's	21 (24.71)	18.2507
2000's	38 (44.71)	29.6817
2010's	12 (14.12)	24.3611
2020's	4 (4.71)	2.80

Authors

Authors	Studies
Cosson, A; Gacon, G; Krishnamoorthy, R; Labie, D; Tapon, J; Wajcman, H	1
Bechtel, KC; Bonaventura, C; Bonaventura, J; Dunlap, WM; Johnson, MH; Jue, DL; Moo-Penn, WF; Opella, SJ; Schmidt, DE; Schmidt, RM	1
Cutler, RL; Davies, AM; Greenwood, C; Mauk, AG; Moore, GR; Pielak, GJ; Smith, M; Thurgood, AG; Williamson, DJ	1
Koshy, TI; Luntz, TL; Margoliash, E; Schejter, A	1
Atsmon, A; Bomstein, Y; Mamet, R; Mevasser, R; Schoenfeld, N	1
Datta, K; Shanker, J	1
Beuzard, Y; London, IM; Rodvien, R	1
Meyer, UA; Schmid, R	1
Kaplan, BH; Tricoche, M; Vanderhoff, G	1
Song, H; Swick, RW	1
Guerritore, D; Zito, R	1
Fuhr, JE; Grayzel, AI; London, IM	1
Burnham, BF; Horton, WJ; Kushner, JP; Morton, KA	1
Banci, L; Bertini, I; Bren, KL; Gray, HB; Sompornpisut, P; Turano, P	1
Newmyer, SL; Ortiz de Montellano, PR	1
Deybach, JC; Nordmann, Y; Puy, H	1
Coggins, JR; Kelly, SM; Lindsay, JG; Malarkey, K; McKnight, J; Miles, JS; Munro, AW; Price, NC; Thomson, AJ	1
Banci, L; Bertini, I; Ferrer, JC; Mauk, AG; Morris, IK; Smith, KM; Smith, M; Turano, P	1
Bren, KL; Casimiro, DR; Gray, HB; Lu, Y; Richards, JH	1
Balasubramanian, S; Boxer, SG; Lambright, DG	1
Buse, G; Hildebrandt, P; Mauk, AG; Soulimane, T; Vanhecke, F	1
Galactéros, F; Groff, P; Kalmes, G; Kiger, L; Kister, J; Promé, D; Wajcman, H	1
Gugneja, S; Scarpulla, RC; Virbasius, CM	1
Daldal, F; Ding, H; Dutton, PL; Saribaş, AS	1
Crane, BR; Gachhui, R; Ghosh, DK; Parkinson, J; Stuehr, DJ; Wu, C	1
Ferrone, FA; Himanen, JP; Liao, D; Manning, JM; Martin de Llano, JJ	1
Babcock, GT; Marletta, MA; Schelvis, JP; Zhao, Y	1
Alzari, PM; Betzel, C; Fita, I; Herzog, C; Koller, F; Maté, MJ; Nykyri, LM; Zamocky, M	1
Buse, G; Döpner, S; Hildebrandt, P; Mauk, AG; Rosell, FI; Soulimane, T; von Walter, M	1
Boxer, SG; Dawson, JH; Dou, Y; Franzen, S; Hu, R; Ikeda-Saito, M; Ortiz de Montellano, PR; Pond, AE; Roach, MP; Rux, AH; Sono, M; Thomas, MR; Wilks, A; Woodruff, WH	1
Alben, JO; Barquera, B; Brzezinski, P; Gennis, RB; Katsonouri, A; Ma, J; Puustinen, A; Thomas, JW; Tsatsos, PH; Wikström, M; Zaslavsky, D	1
Das, TK; Ferguson-Miller, S; Gennis, RB; Lee, HM; Mills, D; Rousseau, DL	1
Chu, GC; Ikeda-Saito, M; Katakura, K; Kayama, T; Sasahara, M; Sato, M; Sun, D; Tomita, T; Yoshida, T; Zhang, X	1
Ferguson, SJ; Tomlinson, EJ	1
Aono, S; Honma, Y; Kato, T; Miyatake, H; Nakajima, H; Park, SY; Shiro, Y; Tawara, T	1
Ishikawa, H; Ishimori, K; Morishima, I; Takahashi, S; Uchida, T	1
Bhattacharya, S; Falzone, CJ; Lecomte, JT; Scott, NL; Vu, BC; Wang, Y	1
Estabrook, RW; Gilep, AA; Guryev, OL; Usanov, SA	1
Gennis, RB; Hellwig, P; Huang , HW; Konstantinov, AA; Moënne-Loccoz, P; Osborne, JP; Zhang, J	1
Arese, M; Brown, K; Brunori, M; Cambillau, C; Cutruzzola', F; Roig-Zamboni, V; Sun, W; Tegoni, M	1
Borisov, VB; Gennis, RB; Konstantinov, AA; Liebl, U; Martin, JL; Rappaport, F; Vos, MH; Zhang, J	1
Banci, L; Bertini, I; Cavallaro, G; Luchinat, C	1
Asokan, A; de Ropp, JS; La Mar, GN; Newmyer, S; Ortiz de Montellano, PR; Sham, S	1
Littlejohn, TK; Takikawa, O; Truscott, RJ; Walker, MJ	1
Chen, JJ; Han, AP; Rafie-Kolpin, M	1
Ahuja, U; Thöny-Meyer, L	1
Chapman, SK; Miles, CS; Mowat, CG; Reid, GA; Rothery, EL; Walkinshaw, MD	1
Ferguson, SJ; Redfield, C; Smith, LJ; Wain, R	1
Babcock, GT; Durham, B; Ferguson-Miller, S; Geren, L; Hiser, C; Hoganson, CW; Millett, F; Mills, DA; Qian, J; Schmidt, B; Wang, K	1
Hira, S; Igarashi, K; Ikeda-Saito, M; Sun, J; Suzuki, H; Tashiro, S; Yamazaki, C; Yoshida, M; Zenke, Y	1
Falzone, CJ; Lecomte, JT; Nothnagel, HJ; Vu, BC; Vuletich, DA	1
Banerjee, R; Zou, CG	1
Ishimori, K; O'Brian, MR; Yang, J	1
Blobaum, AL; Harris, DL; Hollenberg, PF	1
Rothkegel, C; Schmidt, PM; Schröder, H; Stasch, JP; Wunder, F	1
Bryson, TA; Davydov, R; Dawson, JH; Hoffman, BM; Jin, S; Kim, SH; Perera, R; Sono, M; Yang, TC	1
McLean, KJ; Mewies, M; Munro, AW; Papadopoulou, ND; Raven, EL; Seward, HE; Svistunenko, DA	1
Borel, F; de Groot, A; de Rosny, E; Fontecilla-Camps, JC; Gaillard, J; Jouve, HM; Jullian-Binard, C; Pebay-Peyroula, E	1
Knappenberger, JA; Kuriakose, SA; Lecomte, JT; Nothnagel, HJ; Vu, BC; Vuletich, DA	1
Jaffer, N; Jia, Z; Suits, MD	1
Girvan, HM; Heyes, DJ; Munro, AW; Scrutton, NS	1
Beeghley, CA; Graf, CB; Liang, Q; Miller, GT; Timkovich, R	1
Aranda, R; Dooley, DM; Fabian, M; Lei, B; Liu, M; Olson, JS; Phillips, GN; Ran, Y; Zhu, H	1
Cryle, MJ; De Voss, JJ	1
Elliott, JL; Haller, RG; Leary, SC; Pierrel, F; Romain, N; Son, M; Winge, DR	1
Inada, A; Ozaki, S; Sada, K	1
Bowler, BE; Kurchan, E; Roder, H; Tzul, FO	1
Kobayashi, K; Mogi, T; Tagawa, S	1
Gorres, KL; Pua, KH; Raines, RT	1
da Silva, GF; Kulmacz, RJ; Liu, W; Palmer, G; Tsai, AL; Wu, G	1
Baskaran, P; Beuve, A; Heckler, EJ; van den Akker, F	1
Bowler, BE; Khan, MK	1
Bowler, BE; Cherney, MM; Junior, CC	1
Bhagi-Damodaran, A; Lu, Y; Marshall, NM; Petrik, ID; Robinson, H	1
Bren, KL; Elliott, SJ; Levin, BD; Sullivan, KK; Walsh, KA	1
Ferguson, SJ; Redfield, C; Smith, LJ; Tozawa, K	1
Battaile, KP; Im, W; Kumar, R; Lovell, S; Matsumura, H; Moënne-Loccoz, P; Qi, Y; Rivera, M; Yao, H	1
Battista, T; Cervelli, M; Ciaccio, C; Coletta, M; Fiorucci, L; Howes, BD; Mariottini, P; Santucci, R; Smulevich, G; Tognaccini, L	1
Beattie, AD; Benaragama, I; Meesapyodsuk, D; Qiu, X	1
Basran, J; Carr, KH; Kwon, H; Lad, L; Moody, PCE; Raven, EL; Turner, DD	1
Bruegger, JJ; Guo, Y; Hespen, CW; Marletta, MA	1
Bald, D; Gennis, RB; Goojani, HG; Hakvoort, H; Hong, S; Konings, J; Lill, H; Sakamoto, J	1
Ben Aoun, S; Ibrahim, SM; Kooli, F; Nakajima, H; Watanabe, Y	1
Ferguson-Miller, S; Garavito, RM; Hall, R; Hiser, C; Li, F; Liu, J	1
Ben Aoun, S; Ibrahim, SM	1

Reviews

4 review(s) available for alanine and heme

Article	Year
Intermittent acute porphyria: the enzymatic defect. Research publications - Association for Research in Nervous and Mental Disease, 1974, Volume: 53 Topics: 5-Aminolevulinate Synthetase; Adenosine Triphosphatases; Alanine; Aminolevulinic Acid; Ammonia-Lyases; Dysautonomia, Familial; Heme; Humans; Liver; Porphobilinogen; Porphyrias; Porphyrins	1974
Turnover rates of various muscle proteins. Journal of animal science, 1974, Volume: 38, Issue:5 Topics: Actins; Alanine; Amino Acids; Amino Acyl-tRNA Synthetases; Animals; Arginine; Carbon Radioisotopes; Carbonates; Female; Glutamates; Heme; Isotope Labeling; Levulinic Acids; Liver; Lysosomes; Male; Methylhistidines; Muscle Proteins; Myosins; Nitrogen; Rats; RNA, Messenger; Swine	1974
[Hepatic porphyrias and drugs]. Gastroenterologie clinique et biologique, 1994, Volume: 18, Issue:4 Topics: Acute Disease; Alanine; Arginine; Carbohydrates; Heme; Humans; Ligases; Porphyrias, Hepatic	1994
Redox regulation and reaction mechanism of human cystathionine-beta-synthase: a PLP-dependent hemesensor protein. Archives of biochemistry and biophysics, 2005, Jan-01, Volume: 433, Issue:1 Topics: Alanine; Allosteric Regulation; Amino Acid Motifs; Amino Acid Sequence; Amino Acid Substitution; Animals; Binding Sites; Crystallography, X-Ray; Cystathionine beta-Synthase; DNA Mutational Analysis; Enzyme Activation; Heme; Hemeproteins; Humans; Kinetics; Models, Chemical; Models, Molecular; Models, Structural; Molecular Sequence Data; Molecular Structure; Molecular Weight; Oxidation-Reduction; Protein Binding; Protein Structure, Tertiary; Pyridoxal Phosphate; Sequence Homology, Amino Acid; Substrate Specificity; Threonine	2005

Other Studies

81 other study(ies) available for alanine and heme

Article	Year
Hemoglobin Djelfa beta98 (FG 5) Val leads to Ala: isolation and functional properties of the heme saturated form. Biochimica et biophysica acta, 1977, Jan-25, Volume: 490, Issue:1 Topics: Alanine; Diphosphoglyceric Acids; Erythrocytes; Heme; Hemoglobins, Abnormal; Humans; Hydrogen-Ion Concentration; Oxyhemoglobins; Valine	1977
Hemoglobin Raleigh (beta1 valine replaced by acetylalanine). Structural and functional characterization. Biochemistry, 1977, Nov-01, Volume: 16, Issue:22 Topics: Adult; Alanine; Amino Acids; Carbon Monoxide; Female; Heme; Hemoglobin A; Hemoglobins, Abnormal; Humans; Hydrogen-Ion Concentration; Kinetics; Magnetic Resonance Spectroscopy; Male; Mass Spectrometry; Oxygen; Pedigree; Peptide Fragments; Phytic Acid; Valine	1977
Change in charge of an unvaried heme contact residue does not cause a major change of conformation in cytochrome c. FEBS letters, 1991, Jun-24, Volume: 284, Issue:2 Topics: Alanine; Arginine; Cytochrome c Group; Electrochemistry; Heme; Isoleucine; Leucine; Magnetic Resonance Spectroscopy; Mutagenesis; Protein Conformation; Saccharomyces cerevisiae	1991
Changing the invariant proline-30 of rat and Drosophila melanogaster cytochromes c to alanine or valine destabilizes the heme crevice more than the overall conformation. Proceedings of the National Academy of Sciences of the United States of America, 1990, Volume: 87, Issue:22 Topics: Alanine; Animals; Binding Sites; Cloning, Molecular; Cytochrome c Group; Drosophila melanogaster; Heme; Hot Temperature; Proline; Protein Conformation; Rats; Recombinant Proteins; Spectrum Analysis; Structure-Activity Relationship; Urea; Valine	1990
L-Alanine: 4,5-dioxovalerate transaminase does not regulate heme synthesis in rat liver. Biochimica et biophysica acta, 1990, May-16, Volume: 1034, Issue:2 Topics: Alanine; Allylisopropylacetamide; Aminolevulinic Acid; Animals; Chick Embryo; Dicarbethoxydihydrocollidine; Enzyme Induction; Heme; Hemin; Liver; Male; Phenobarbital; Porphyrins; Rats; Rats, Inbred Strains; Transaminases; Valerates	1990
Evidence of hemin as an end product inhibitor of L-alanine: 4,5-dioxovalerate transaminase in rat liver mitochondria. FEBS letters, 1985, Sep-09, Volume: 189, Issue:1 Topics: Alanine; Animals; Binding, Competitive; Dose-Response Relationship, Drug; Heme; Hemin; Kinetics; Male; Mitochondria, Liver; Rats; Rats, Inbred Strains; Time Factors; Transaminases; Valerates	1985
Effect of hemin on the synthesis of hemoglobin and other proteins in mammalian cells. Proceedings of the National Academy of Sciences of the United States of America, 1973, Volume: 70, Issue:4 Topics: Alanine; Animals; Carbon Isotopes; Carbonic Anhydrases; Carcinoma, Krebs 2; Cell Line; Chromatography; Chromatography, Ion Exchange; Electrophoresis, Polyacrylamide Gel; Globins; Heme; Hemoglobins; In Vitro Techniques; Neoplasm Proteins; Protein Biosynthesis; Rabbits; Reticulocytes; RNA, Messenger	1973
Regulatory role of heme. Annals of the New York Academy of Sciences, 1974, Nov-29, Volume: 241, Issue:0 Topics: Alanine; Animals; Antigen-Antibody Reactions; Glutathione; Guinea Pigs; Heme; Hemoglobins; Kinetics; Mice; Peptide Chain Initiation, Translational; Peptide Initiation Factors; Protein Biosynthesis; Rabbits; Reticulocytes; Ribosomes; RNA, Messenger; Sheep; Species Specificity; Time Factors; Tritium	1974
The terminal groups of chlorocruorin. Biochimica et biophysica acta, 1971, Mar-23, Volume: 229, Issue:3 Topics: Alanine; Amino Acid Sequence; Animals; Annelida; Arginine; Carboxypeptidases; Glutamates; Heme; Hemolymph; Histidine; Microscopy, Electron; Molecular Weight; Nitrobenzenes; Peptides; Proteins; Tyrosine	1971
Effects of inhibitors of protein synthesis on the synthesis of heme in rabbit reticulocytes. Biochemical and biophysical research communications, 1967, Sep-07, Volume: 28, Issue:5 Topics: Alanine; Animals; Blood Proteins; Carbon Isotopes; Cycloheximide; Globins; Glycine; Heme; Puromycin; Rabbits; Reticulocytes; Spectrophotometry	1967
Biosynthesis of porphyrins and heme from gamma, delta-dioxovalerate by intact hepatocytes. Proceedings of the National Academy of Sciences of the United States of America, 1981, Volume: 78, Issue:9 Topics: Alanine; Aminolevulinic Acid; Animals; Cells, Cultured; Glycine; Heme; Keto Acids; Levulinic Acids; Liver; Male; Porphyrins; Rats; Succinates; Succinic Acid; Valerates	1981
Three-dimensional solution structure of the cyanide adduct of a Met80Ala variant of Saccharomyces cerevisiae iso-1-cytochrome c. Identification of ligand-residue interactions in the distal heme cavity. Biochemistry, 1995, Sep-12, Volume: 34, Issue:36 Topics: Alanine; Amino Acid Sequence; Animals; Crystallography, X-Ray; Cyanides; Cytochrome c Group; Cytochromes c; Heme; Horses; Ligands; Magnetic Resonance Spectroscopy; Methionine; Molecular Sequence Data; Myocardium; Protein Conformation; Protein Structure, Secondary; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Solutions	1995
Horseradish peroxidase His-42 --> Ala, His-42 --> Val, and Phe-41 --> Ala mutants. Histidine catalysis and control of substrate access to the heme iron. The Journal of biological chemistry, 1995, Aug-18, Volume: 270, Issue:33 Topics: Alanine; Animals; Catalysis; Cell Line; Heme; Histidine; Horseradish Peroxidase; Imines; Iron; Kinetics; Mutagenesis, Site-Directed; Phenylalanine; Recombinant Proteins; Spectrum Analysis; Spodoptera; Substrate Specificity; Sulfides; Sulfoxides; Valine	1995
The role of tryptophan 97 of cytochrome P450 BM3 from Bacillus megaterium in catalytic function. Evidence against the 'covalent switching' hypothesis of P-450 electron transfer. The Biochemical journal, 1994, Oct-15, Volume: 303 ( Pt 2) Topics: Alanine; Bacillus megaterium; Bacterial Proteins; Base Sequence; Catalysis; Circular Dichroism; Cytochrome P-450 Enzyme System; DNA Primers; Electron Spin Resonance Spectroscopy; Electron Transport; Escherichia coli; Heme; Mixed Function Oxygenases; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; NADPH-Ferrihemoprotein Reductase; Phenylalanine; Protein Structure, Secondary; Spectrophotometry, Ultraviolet; Tryptophan; Tyrosine	1994
Active site coordination chemistry of the cytochrome c peroxidase Asp235Ala variant: spectroscopic and functional characterization. Biochemistry, 1994, Jun-28, Volume: 33, Issue:25 Topics: Alanine; Aspartic Acid; Base Sequence; Binding Sites; Cytochrome-c Peroxidase; Electron Spin Resonance Spectroscopy; Heme; Histidine; Hydrogen Bonding; Hydrogen-Ion Concentration; Iron; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Recombinant Proteins; Spectrum Analysis; Structure-Activity Relationship; Temperature; Tryptophan	1994
Structurally engineered cytochromes with unusual ligand-binding properties: expression of Saccharomyces cerevisiae Met-80-->Ala iso-1-cytochrome c. Proceedings of the National Academy of Sciences of the United States of America, 1993, Dec-15, Volume: 90, Issue:24 Topics: Alanine; Amino Acid Sequence; Animals; Base Sequence; Binding Sites; Cloning, Molecular; Cytochrome c Group; Cytochromes; Cytochromes c; Escherichia coli; Heme; Horses; Methionine; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Protein Conformation; Protein Engineering; Recombinant Proteins; Restriction Mapping; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Transcription, Genetic	1993
Dynamics of protein relaxation in site-specific mutants of human myoglobin. Biochemistry, 1993, Sep-28, Volume: 32, Issue:38 Topics: Alanine; Amino Acid Sequence; Cysteine; Heme; Humans; Kinetics; Mathematics; Mutagenesis, Site-Directed; Myoglobin; Protein Conformation; Recombinant Proteins; Spectrophotometry; Time Factors	1993
Resonance Raman study of the interactions between cytochrome c variants and cytochrome c oxidase. Biochemistry, 1993, Oct-12, Volume: 32, Issue:40 Topics: Alanine; Amino Acid Sequence; Animals; Binding Sites; Cattle; Cytochrome c Group; Cytochromes c; Electron Transport Complex IV; Heme; Horses; Models, Molecular; Mutagenesis, Site-Directed; Protein Conformation; Recombinant Proteins; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Spectrum Analysis, Raman	1993
Hb J-Europa [beta 62(E6)Ala-->Asp]: normal oxygen binding properties in a new variant involving a residue located distal to the heme. Hemoglobin, 1996, Volume: 20, Issue:2 Topics: Adult; Alanine; Asparagine; Heme; Hemoglobins; Hemoglobins, Abnormal; Humans; Hydrolysis; Male; Mutation; Oxygen	1996
Nuclear respiratory factors 1 and 2 utilize similar glutamine-containing clusters of hydrophobic residues to activate transcription. Molecular and cellular biology, 1996, Volume: 16, Issue:10 Topics: Alanine; Amino Acid Sequence; Animals; Base Sequence; COS Cells; DNA Primers; DNA-Binding Proteins; DNA, Mitochondrial; Fungal Proteins; Glutamine; Heme; Leucine Zippers; Molecular Sequence Data; Mutagenesis, Site-Directed; NF-E2-Related Factor 1; NF-E2-Related Factor 2; Nuclear Respiratory Factors; Polymerase Chain Reaction; Recombinant Fusion Proteins; Respiration; Saccharomyces cerevisiae Proteins; Sequence Deletion; Structure-Activity Relationship; Trans-Activators; Transcription Factors; Transcription, Genetic; Transcriptional Activation; Transfection	1996
Substitutions at position 146 of cytochrome b affect drastically the properties of heme bL and the Qo site of Rhodobacter capsulatus cytochrome bc1 complex. Biochimica et biophysica acta, 1997, Mar-28, Volume: 1319, Issue:1 Topics: Alanine; Amino Acid Sequence; Cytochrome b Group; Electron Spin Resonance Spectroscopy; Electron Transport Complex III; Glycine; Heme; Kinetics; Membrane Proteins; Molecular Sequence Data; Mutagenesis, Site-Directed; Rhodobacter capsulatus; Structure-Activity Relationship; Ubiquinone; Valine	1997
Mutagenesis of acidic residues in the oxygenase domain of inducible nitric-oxide synthase identifies a glutamate involved in arginine binding. Biochemistry, 1997, Apr-29, Volume: 36, Issue:17 Topics: Alanine; Amino Acid Sequence; Animals; Antioxidants; Arginine; Biopterins; Cattle; Chromatography, Gel; Glutamic Acid; Heme; Humans; Mice; Molecular Sequence Data; Mutagenesis, Site-Directed; Nitric Oxide Synthase; Oxygenases; Rats; Structure-Activity Relationship	1997
Solubility of sickle hemoglobin measured by a kinetic micromethod. Biophysical journal, 1996, Volume: 70, Issue:5 Topics: Alanine; Carboxyhemoglobin; Heme; Hemoglobin A; Hemoglobin, Sickle; Humans; Kinetics; Leucine; Microchemistry; Models, Chemical; Photolysis; Point Mutation; Solubility; Thermodynamics	1996
Identification of histidine 105 in the beta1 subunit of soluble guanylate cyclase as the heme proximal ligand. Biochemistry, 1998, Mar-31, Volume: 37, Issue:13 Topics: Alanine; Escherichia coli; Guanylate Cyclase; Heme; Histidine; Imidazoles; Ligands; Mutagenesis, Site-Directed; Solubility; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman	1998
Structure of catalase-A from Saccharomyces cerevisiae. Journal of molecular biology, 1999, Feb-12, Volume: 286, Issue:1 Topics: Alanine; Binding Sites; Catalase; Crystallography, X-Ray; Heme; Models, Molecular; Mutagenesis, Site-Directed; NADP; Protein Conformation; Saccharomyces cerevisiae; Valine	1999
The structural and functional role of lysine residues in the binding domain of cytochrome c in the electron transfer to cytochrome c oxidase. European journal of biochemistry, 1999, Volume: 261, Issue:2 Topics: Alanine; Animals; Binding Sites; Cattle; Cytochrome c Group; Electron Transport; Electron Transport Complex IV; Heme; Kinetics; Lysine; Models, Molecular; Mutation; Phospholipids; Polylysine; Protein Conformation; Spectrum Analysis, Raman	1999
Assignment of the heme axial ligand(s) for the ferric myoglobin (H93G) and heme oxygenase (H25A) cavity mutants as oxygen donors using magnetic circular dichroism. Biochemistry, 1999, Jun-08, Volume: 38, Issue:23 Topics: Alanine; Animals; Circular Dichroism; Electron Transport; Glycine; Heme; Heme Oxygenase (Decyclizing); Histidine; Humans; Hydrogen-Ion Concentration; Iron; Ligands; Mutagenesis, Site-Directed; Myoglobin; Oxygen; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman; Titrimetry; Whales	1999
Glutamate-89 in subunit II of cytochrome bo3 from Escherichia coli is required for the function of the heme-copper oxidase. Biochemistry, 1999, Nov-16, Volume: 38, Issue:46 Topics: Alanine; Conserved Sequence; Copper; Cytochrome b Group; Cytochromes; Electron Transport Complex IV; Enzyme Activation; Escherichia coli; Escherichia coli Proteins; Glutamic Acid; Heme; Hydrogen-Ion Concentration; Membrane Proteins; Oxidation-Reduction; Proton Pumps; Quinone Reductases; Spectrophotometry, Ultraviolet; Static Electricity	1999
Mutations in the putative H-channel in the cytochrome c oxidase from Rhodobacter sphaeroides show that this channel is not important for proton conduction but reveal modulation of the properties of heme a. Biochemistry, 2000, Mar-21, Volume: 39, Issue:11 Topics: Alanine; Amino Acid Sequence; Amino Acid Substitution; Animals; Arginine; Cattle; Electron Transport Complex IV; Enzyme Activation; Glutamine; Heme; Histidine; Lysine; Molecular Sequence Data; Mutagenesis, Site-Directed; Proton Pumps; Rhodobacter sphaeroides; Spectrum Analysis, Raman; Tyrosine	2000
Histidine 20, the crucial proximal axial heme ligand of bacterial heme oxygenase Hmu O from Corynebacterium diphtheriae. The Journal of biological chemistry, 2000, Jun-09, Volume: 275, Issue:23 Topics: Alanine; Amino Acid Sequence; Amino Acid Substitution; Ascorbic Acid; Bacterial Proteins; Base Sequence; Corynebacterium diphtheriae; Electron Spin Resonance Spectroscopy; Heme; Heme Oxygenase (Decyclizing); Histidine; Ligands; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Spectrophotometry; Spectrum Analysis, Raman	2000
Conversion of a c type cytochrome to a b type that spontaneously forms in vitro from apo protein and heme: implications for c type cytochrome biogenesis and folding. Proceedings of the National Academy of Sciences of the United States of America, 2000, May-09, Volume: 97, Issue:10 Topics: Alanine; Amino Acid Substitution; Apoproteins; Cystine; Cytochrome b Group; Cytochrome c Group; Escherichia coli; Genetic Variation; Guanidine; Heme; Hydrogen-Ion Concentration; Kinetics; Mutagenesis, Site-Directed; Oxidation-Reduction; Protein Denaturation; Protein Folding; Recombinant Proteins; Thermodynamics	2000
Redox properties and coordination structure of the heme in the co-sensing transcriptional activator CooA. The Journal of biological chemistry, 2001, Mar-09, Volume: 276, Issue:10 Topics: Alanine; Bacterial Proteins; Cysteine; Electrochemistry; Escherichia coli Proteins; Fimbriae Proteins; Heme; Histidine; Iron; Ligands; Models, Chemical; Mutagenesis, Site-Directed; Oxidation-Reduction; Oxygen; Spectrum Analysis, Raman; Transcriptional Activation	2001
Ligand migration in human myoglobin: steric effects of isoleucine 107(G8) on O(2) and CO binding. Biophysical journal, 2001, Volume: 80, Issue:3 Topics: Alanine; Amino Acid Substitution; Binding Sites; Heme; Humans; Isoleucine; Kinetics; Leucine; Ligands; Models, Molecular; Mutagenesis, Site-Directed; Myoglobin; Phenylalanine; Protein Conformation; Recombinant Proteins; Thermodynamics; Valine	2001
Structural and dynamic perturbations induced by heme binding in cytochrome b5. Biochemistry, 2001, Apr-17, Volume: 40, Issue:15 Topics: Alanine; Amino Acid Substitution; Animals; Apoproteins; Carbon Monoxide; Crystallography, X-Ray; Cytochrome b Group; Cytochromes b; Cytochromes b5; Heme; Histidine; Macromolecular Substances; Methylamines; Nuclear Magnetic Resonance, Biomolecular; Oxidants; Oxidation-Reduction; Protein Binding; Protein Conformation; Protein Denaturation; Protein Folding; Rats; Thermodynamics	2001
Interaction of apo-cytochrome b5 with cytochromes P4503A4 and P45017A: relevance of heme transfer reactions. Biochemistry, 2001, Apr-24, Volume: 40, Issue:16 Topics: Alanine; Animals; Apoproteins; Aryl Hydrocarbon Hydroxylases; Catalysis; Chromatography, Affinity; Cytochrome b Group; Cytochrome P-450 CYP3A; Cytochrome P-450 Enzyme System; Cytochromes b; Electron Transport; Enzymes, Immobilized; Heme; Histidine; Holoenzymes; Horses; Humans; Kinetics; Mixed Function Oxygenases; Molecular Weight; Mutagenesis, Site-Directed; Myoglobin; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Rats; Recombinant Proteins; Spectrophotometry; Steroid 17-alpha-Hydroxylase; Steroid Hydroxylases	2001
Site-directed mutation of the highly conserved region near the Q-loop of the cytochrome bd quinol oxidase from Escherichia coli specifically perturbs heme b595. Biochemistry, 2001, Jul-24, Volume: 40, Issue:29 Topics: Alanine; Amino Acid Sequence; Carbon Monoxide; Conserved Sequence; Cyanides; Cytochrome b Group; Cytochromes; Electrochemistry; Electron Spin Resonance Spectroscopy; Electron Transport Chain Complex Proteins; Escherichia coli; Escherichia coli Proteins; Glutamic Acid; Heme; Molecular Sequence Data; Mutagenesis, Site-Directed; Oxidation-Reduction; Oxidoreductases; Oxidoreductases, N-Demethylating; Protein Binding; Protein Structure, Tertiary; Quinone Reductases; Spectrophotometry, Ultraviolet; Spectroscopy, Fourier Transform Infrared; Spectrum Analysis, Raman	2001
Domain swing upon His to Ala mutation in nitrite reductase of Pseudomonas aeruginosa. Journal of molecular biology, 2001, Sep-21, Volume: 312, Issue:3 Topics: Alanine; Amino Acid Substitution; Binding Sites; Crystallization; Crystallography, X-Ray; Dimerization; Heme; Histidine; Models, Molecular; Mutation; Nitric Oxide; Nitrite Reductases; Pliability; Protein Structure, Quaternary; Protein Structure, Tertiary; Pseudomonas aeruginosa; Spectrophotometry; Static Electricity	2001
Interactions between heme d and heme b595 in quinol oxidase bd from Escherichia coli: a photoselection study using femtosecond spectroscopy. Biochemistry, 2002, Feb-05, Volume: 41, Issue:5 Topics: Alanine; Amino Acid Substitution; Animals; Binding Sites; Carbon Monoxide; Cell Membrane; Escherichia coli; Glutamic Acid; Heme; Mutagenesis, Site-Directed; Myoglobin; Oxidation-Reduction; Oxidoreductases; Oxygen; Photolysis; Protein Binding; Spectrophotometry; Spectrophotometry, Ultraviolet	2002
Chemical shift-based constraints for solution structure determination of paramagnetic low-spin heme proteins with bis-His and His-CN axial ligands: the cases of oxidized cytochrome b(5) and Met80Ala cyano-cytochrome c. Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2002, Volume: 7, Issue:4-5 Topics: Alanine; Cyanides; Cytochrome c Group; Cytochromes b5; Heme; Histidine; Ligands; Methionine; Models, Molecular; Molecular Structure; Mutation; Oxidation-Reduction; Yeasts	2002
Influence of the distal his in imparting imidazolate character to the proximal his in heme peroxidase: (1)h NMR spectroscopic study of cyanide-inhibited his42-->ala horseradish peroxidase. Journal of the American Chemical Society, 2002, Sep-18, Volume: 124, Issue:37 Topics: Alanine; Cyanides; Enzyme Inhibitors; Heme; Histidine; Horseradish Peroxidase; Hydrogen Bonding; Imidazoles; Nuclear Magnetic Resonance, Biomolecular; Peroxidases; Protein Conformation	2002
Asp274 and his346 are essential for heme binding and catalytic function of human indoleamine 2,3-dioxygenase. The Journal of biological chemistry, 2003, Aug-08, Volume: 278, Issue:32 Topics: Alanine; Amino Acid Sequence; Animals; Aspartic Acid; Blotting, Western; Catalysis; Cell Division; Circular Dichroism; Cytokines; Electron Spin Resonance Spectroscopy; Electrophoresis, Polyacrylamide Gel; Heme; Histidine; Humans; Indoleamine-Pyrrole 2,3,-Dioxygenase; Interferon-gamma; Kinetics; Ligands; Mice; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Plasmids; Protein Binding; Protein Conformation; Rats; Sequence Homology, Amino Acid; Tryptophan; Tryptophan Oxygenase; Ultraviolet Rays; Up-Regulation	2003
Autophosphorylation of threonine 485 in the activation loop is essential for attaining eIF2alpha kinase activity of HRI. Biochemistry, 2003, Jun-03, Volume: 42, Issue:21 Topics: Alanine; Amino Acid Sequence; Aspartic Acid; Blotting, Western; Cell Line; Chromatography, Thin Layer; Dose-Response Relationship, Drug; eIF-2 Kinase; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Eukaryotic Initiation Factor-2; Heme; Hemin; Humans; Models, Biological; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Peptides; Phosphorylation; Protein Structure, Tertiary; Threonine; Trypsin	2003
Dynamic features of a heme delivery system for cytochrome C maturation. The Journal of biological chemistry, 2003, Dec-26, Volume: 278, Issue:52 Topics: Alanine; Amino Acid Motifs; Bacterial Outer Membrane Proteins; Bacterial Proteins; Cell Division; Cytochromes c; Cytoplasm; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Escherichia coli Proteins; Genotype; Heme; Hemeproteins; Histidine; Membrane Proteins; Models, Biological; Mutagenesis; Mutagenesis, Site-Directed; Mutation; Oligonucleotides; Periplasm; Phenotype; Plasmids; Precipitin Tests; Protein Binding; Subcellular Fractions; Tryptophan	2003
Histidine 61: an important heme ligand in the soluble fumarate reductase from Shewanella frigidimarina. Biochemistry, 2003, Nov-18, Volume: 42, Issue:45 Topics: Alanine; Crystallization; Crystallography, X-Ray; Cytochrome c Group; Deuterium Oxide; Electron Transport; Flavin-Adenine Dinucleotide; Heme; Histidine; Kinetics; Ligands; Methionine; Molecular Weight; Mutagenesis, Site-Directed; Potentiometry; Shewanella; Solubility; Solvents; Succinate Dehydrogenase	2003
NMR analysis shows that a b-type variant of Hydrogenobacter thermophilus cytochrome c552 retains its native structure. The Journal of biological chemistry, 2004, Apr-09, Volume: 279, Issue:15 Topics: Alanine; Amino Acid Sequence; Bacteria, Aerobic; Cysteine; Cytochrome c Group; Heme; Hydrogen; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Methionine; Models, Molecular; Molecular Sequence Data; Mutagenesis; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Protons; Temperature	2004
Role of the conserved arginine pair in proton and electron transfer in cytochrome C oxidase. Biochemistry, 2004, May-18, Volume: 43, Issue:19 Topics: Alanine; Arginine; Catalysis; Conserved Sequence; Electron Spin Resonance Spectroscopy; Electron Transport; Electron Transport Complex IV; Enzyme Activation; Glutamine; Heme; Kinetics; Lysine; Magnesium; Mutagenesis, Site-Directed; Photolysis; Proline; Proton Pumps; Rhodobacter sphaeroides; Spectrophotometry, Ultraviolet	2004
Heme regulates gene expression by triggering Crm1-dependent nuclear export of Bach1. The EMBO journal, 2004, Jul-07, Volume: 23, Issue:13 Topics: Active Transport, Cell Nucleus; Alanine; Amino Acid Motifs; Amino Acid Sequence; Amino Acid Substitution; Basic-Leucine Zipper Transcription Factors; Cell Line; Cell Nucleus; Chromatin Immunoprecipitation; Dimerization; DNA-Binding Proteins; Erythroid-Specific DNA-Binding Factors; Escherichia coli; Exportin 1 Protein; Fanconi Anemia Complementation Group Proteins; Fibroblasts; Gene Expression Regulation; Genes, Reporter; Globins; Glutathione Transferase; Green Fluorescent Proteins; Heme; Heme Oxygenase (Decyclizing); Heme Oxygenase-1; Hemin; Humans; Immunohistochemistry; Karyopherins; Leucine Zippers; MafK Transcription Factor; Membrane Proteins; Molecular Sequence Data; Nuclear Proteins; Plasmids; Receptors, Cytoplasmic and Nuclear; Recombinant Fusion Proteins; Repressor Proteins; Spectrophotometry; Transcription Factors; Transcription, Genetic; Zinc Fingers	2004
Cyanide binding to hexacoordinate cyanobacterial hemoglobins: hydrogen-bonding network and heme pocket rearrangement in ferric H117A Synechocystis hemoglobin. Biochemistry, 2004, Oct-05, Volume: 43, Issue:39 Topics: Alanine; Bacterial Proteins; Binding Sites; Cyanobacteria; Heme; Hemeproteins; Hemoglobins; Histidine; Hot Temperature; Hydrogen Bonding; Imidazoles; Iron; Mutagenesis, Site-Directed; Nitrogen Isotopes; Nuclear Magnetic Resonance, Biomolecular; Potassium Cyanide; Protein Binding; Protein Denaturation; Recombinant Proteins; Truncated Hemoglobins	2004
Two heme binding sites are involved in the regulated degradation of the bacterial iron response regulator (Irr) protein. The Journal of biological chemistry, 2005, Mar-04, Volume: 280, Issue:9 Topics: Alanine; Amino Acid Motifs; Bacterial Proteins; Binding Sites; Bradyrhizobium; Ferrochelatase; Glutathione Transferase; Heme; Histidine; Iron; Mutagenesis; Mutagenesis, Site-Directed; Mutation; Oxidation-Reduction; Oxygen; Protein Structure, Tertiary; Recombinant Fusion Proteins; Recombinant Proteins; Time Factors; Transcription Factors	2005
P450 active site architecture and reversibility: inactivation of cytochromes P450 2B4 and 2B4 T302A by tert-butyl acetylenes. Biochemistry, 2005, Mar-15, Volume: 44, Issue:10 Topics: Alanine; Alkynes; Animals; Aryl Hydrocarbon Hydroxylases; Binding Sites; Catalysis; Chromatography, High Pressure Liquid; Cytochrome P450 Family 2; Enzyme Inhibitors; Ethers; Heme; Hydrogen Bonding; Models, Molecular; Oxidants; Peroxides; Rabbits; Spectrometry, Fluorescence; Spectrometry, Mass, Electrospray Ionization; Threonine	2005
Residues stabilizing the heme moiety of the nitric oxide sensor soluble guanylate cyclase. European journal of pharmacology, 2005, Apr-18, Volume: 513, Issue:1-2 Topics: Alanine; Amino Acid Sequence; Amino Acid Substitution; Animals; Benzoates; Binding Sites; CHO Cells; Cricetinae; Cricetulus; Cyclic GMP; Diethylamines; Dose-Response Relationship, Drug; Enzyme Activation; Enzyme Inhibitors; Genotype; Guanylate Cyclase; Heme; Molecular Sequence Data; Mutation, Missense; Nitric Acid; Nitrogen Oxides; Oxadiazoles; Protoporphyrins; Pyrazoles; Pyridines; Quinoxalines; Sequence Homology, Amino Acid; Serine; Solubility; Transfection	2005
Cryoreduction EPR and 13C, 19F ENDOR study of substrate-bound substates and solvent kinetic isotope effects in the catalytic cycle of cytochrome P450cam and its T252A mutant. Dalton transactions (Cambridge, England : 2003), 2005, Nov-07, Issue:21 Topics: Alanine; Camphor 5-Monooxygenase; Carbon Isotopes; Catalysis; Electron Spin Resonance Spectroscopy; Fluorine; Heme; Iron; Kinetics; Models, Molecular; Mutant Proteins; Mutation; Oxidation-Reduction; Oxygen; Protein Binding; Protein Structure, Tertiary; Solvents; Substrate Specificity; Threonine	2005
Redox and spectroscopic properties of human indoleamine 2,3-dioxygenase and a His303Ala variant: implications for catalysis. Biochemistry, 2005, Nov-01, Volume: 44, Issue:43 Topics: Alanine; Binding Sites; Catalysis; Ferric Compounds; Ferrous Compounds; Genetic Variation; Heme; Histidine; Humans; Hydrogen-Ion Concentration; Indoleamine-Pyrrole 2,3,-Dioxygenase; Ligands; Oxidation-Reduction; Spectrophotometry; Temperature	2005
Drosophila nuclear receptor E75 is a thiolate hemoprotein. Biochemistry, 2006, Aug-15, Volume: 45, Issue:32 Topics: Alanine; Amino Acid Sequence; Animals; Cysteine; DNA-Binding Proteins; Drosophila melanogaster; Drosophila Proteins; Electron Spin Resonance Spectroscopy; Gene Expression; Heme; Hemeproteins; Histidine; Humans; Ligands; Molecular Sequence Data; Mutation; Protein Binding; Protein Structure, Tertiary; Receptors, Cytoplasmic and Nuclear; Sequence Alignment; Solubility; Spectrophotometry, Ultraviolet; Sulfur; Transcription Factors	2006
Proximal influences in two-on-two globins: effect of the Ala69Ser replacement on Synechocystis sp. PCC 6803 hemoglobin. Biochemistry, 2006, Sep-26, Volume: 45, Issue:38 Topics: Alanine; Amino Acid Sequence; Amino Acid Substitution; Cyanides; Ferric Compounds; Globins; Heme; Histidine; Hydrogen-Ion Concentration; Kinetics; Molecular Sequence Data; Myoglobin; Nuclear Magnetic Resonance, Biomolecular; Protein Binding; Protein Denaturation; Recombinant Proteins; Serine; Sperm Whale; Structure-Activity Relationship; Synechocystis; Temperature; Urea	2006
Structure of the Escherichia coli O157:H7 heme oxygenase ChuS in complex with heme and enzymatic inactivation by mutation of the heme coordinating residue His-193. The Journal of biological chemistry, 2006, Dec-01, Volume: 281, Issue:48 Topics: Alanine; Carbon Monoxide; Catalysis; Chromatography, Gas; Crystallography, X-Ray; Escherichia coli O157; Escherichia coli Proteins; Heme; Heme Oxygenase (Decyclizing); Histidine; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; X-Ray Diffraction	2006
Laser photoexcitation of NAD(P)H induces reduction of P450 BM3 heme domain on the microsecond time scale. Journal of the American Chemical Society, 2007, May-23, Volume: 129, Issue:20 Topics: Alanine; Carbon Monoxide; Coenzymes; Cytochrome P-450 Enzyme System; Heme; Iron; Kinetics; Lasers; Mutation; NAD; Oxidation-Reduction; Photochemistry; Protein Binding; Spectrophotometry; Substrate Specificity; Time Factors	2007
Solution conformation of the His-47 to Ala-47 mutant of Pseudomonas stutzeri ZoBell ferrocytochrome c-551. Biophysical journal, 2007, Sep-01, Volume: 93, Issue:5 Topics: Alanine; Bacterial Proteins; Cytochrome c Group; Cytochromes c; Heme; Histidine; Hydrogen Bonding; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Models, Chemical; Molecular Conformation; Mutation; Oxidation-Reduction; Protein Conformation; Pseudomonas stutzeri; Thermodynamics	2007
Bis-methionine ligation to heme iron in the streptococcal cell surface protein Shp facilitates rapid hemin transfer to HtsA of the HtsABC transporter. The Journal of biological chemistry, 2007, Oct-26, Volume: 282, Issue:43 Topics: Alanine; Amino Acid Substitution; ATP-Binding Cassette Transporters; Binding Sites; Electron Spin Resonance Spectroscopy; Heme; Hemin; Hydrogen-Ion Concentration; Kinetics; Membrane Proteins; Methionine; Models, Biological; Models, Molecular; Protein Binding; Protein Structure, Tertiary; Streptococcus pyogenes	2007
The role of the conserved threonine in P450 BM3 oxygen activation: substrate-determined hydroxylation activity of the Thr268Ala mutant. Chembiochem : a European journal of chemical biology, 2008, Jan-25, Volume: 9, Issue:2 Topics: Alanine; Amino Acid Sequence; Bacillus megaterium; Binding Sites; Catalysis; Cytochrome P-450 Enzyme System; Fatty Acids; Heme; Hydroxylation; Kinetics; Mixed Function Oxygenases; Molecular Sequence Data; Mutation; Oxidation-Reduction; Oxygen; Substrate Specificity; Threonine	2008
Isolated cytochrome c oxidase deficiency in G93A SOD1 mice overexpressing CCS protein. The Journal of biological chemistry, 2008, May-02, Volume: 283, Issue:18 Topics: Alanine; Amino Acid Substitution; Animals; Cytochrome-c Oxidase Deficiency; Electrophoresis, Polyacrylamide Gel; Glycine; Heme; Humans; Kidney; Mice; Mice, Transgenic; Molecular Chaperones; Organ Specificity; Oxidative Phosphorylation; Protein Subunits; Spinal Cord; Superoxide Dismutase	2008
Modulation of cystathionine beta-synthase activity by the Arg-51 and Arg-224 mutations. Bioscience, biotechnology, and biochemistry, 2008, Volume: 72, Issue:9 Topics: Alanine; Amino Acid Sequence; Amino Acid Substitution; Catalysis; Cystathionine; Cystathionine beta-Synthase; Heme; Humans; Kinetics; Models, Molecular; Molecular Sequence Data; Molecular Structure; Mutation; Protein Structure, Secondary; Protein Structure, Tertiary; Pyridoxal Phosphate; Recombinant Proteins	2008
Competition between reversible aggregation and loop formation in denatured iso-1-cytochrome c. Biochemistry, 2009, Jan-20, Volume: 48, Issue:2 Topics: Alanine; Amino Acid Sequence; Amino Acid Substitution; Binding Sites; Cytochromes c; Enzyme Stability; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Isoenzymes; Kinetics; Ligands; Models, Chemical; Molecular Sequence Data; Mutation; Protein Binding; Protein Denaturation; Protein Multimerization; Protein Renaturation; Protein Structure, Secondary; Saccharomyces cerevisiae; Sequence Homology, Amino Acid; Temperature	2009
Intramolecular electron transfer processes in Cu(B)-deficient cytochrome bo studied by pulse radiolysis. Journal of biochemistry, 2009, Volume: 145, Issue:5 Topics: Alanine; Amino Acid Substitution; Copper; Cytochrome b Group; Electron Transport; Escherichia coli; Escherichia coli Proteins; Heme; Histidine; Hydrogen-Ion Concentration; Kinetics; Mutation; Oxidation-Reduction; Potassium Cyanide; Potentiometry; Pulse Radiolysis	2009
Stringency of the 2-His-1-Asp active-site motif in prolyl 4-hydroxylase. PloS one, 2009, Nov-05, Volume: 4, Issue:11 Topics: Alanine; Amino Acid Motifs; Aspartic Acid; Carbon; Catalysis; Catalytic Domain; Collagen; Glycine; Heme; Histidine; Humans; Hydrogen; Iron; Ligands; Procollagen-Proline Dioxygenase	2009
Functional and structural roles of residues in the third extramembrane segment of adrenal cytochrome b561. Biochemistry, 2011, Apr-19, Volume: 50, Issue:15 Topics: Adrenal Glands; Alanine; Amino Acid Sequence; Amino Acid Substitution; Animals; Ascorbic Acid; Cattle; Cell Membrane; Cytochrome b Group; DNA Mutational Analysis; Heme; Humans; Mice; Models, Molecular; Molecular Sequence Data; Protein Conformation	2011
Aspartate 102 in the heme domain of soluble guanylyl cyclase has a key role in NO activation. Biochemistry, 2011, May-24, Volume: 50, Issue:20 Topics: Alanine; Animals; Aspartic Acid; Chlorocebus aethiops; COS Cells; Enzyme Activation; Guanylate Cyclase; Heme; Indazoles; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Nitric Oxide; Protein Structure, Tertiary; Protein Subunits; Rats; Receptors, Cytoplasmic and Nuclear; Sequence Homology, Amino Acid; Soluble Guanylyl Cyclase	2011
Conformational properties of polyglutamine sequences in guanidine hydrochloride solutions. Biophysical journal, 2012, Nov-07, Volume: 103, Issue:9 Topics: Alanine; Amino Acid Sequence; Cytochromes c; Guanidine; Heme; Histidine; Lysine; Molecular Sequence Data; Mutagenesis, Insertional; Peptides; Protein Denaturation; Protein Stability; Protein Structure, Tertiary	2012
Mutation of trimethyllysine 72 to alanine enhances His79-heme-mediated dynamics of iso-1-cytochrome c. Biochemistry, 2013, Feb-05, Volume: 52, Issue:5 Topics: Alanine; Amino Acid Substitution; Cytochromes c; Heme; Hydrogen-Ion Concentration; Kinetics; Lysine; Models, Molecular; Protein Conformation; Protein Denaturation; Protein Stability; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Thermodynamics	2013
Systematic tuning of heme redox potentials and its effects on O2 reduction rates in a designed oxidase in myoglobin. Journal of the American Chemical Society, 2014, Aug-27, Volume: 136, Issue:34 Topics: Alanine; Animals; Binding Sites; Biocatalysis; Copper; Electron Transport Complex IV; Heme; Histidine; Hydrogen Bonding; Male; Models, Molecular; Myoglobin; Oxidation-Reduction; Oxygen; Protein Engineering; Serine; Spermatozoa; Whales	2014
Methionine ligand lability of homologous monoheme cytochromes c. Inorganic chemistry, 2015, Jan-05, Volume: 54, Issue:1 Topics: Alanine; Amino Acid Sequence; Amino Acid Substitution; Bacterial Proteins; Cytochromes c; Electrochemical Techniques; Electrodes; Escherichia coli; Gene Expression; Heme; Histidine; Kinetics; Ligands; Methionine; Molecular Sequence Data; Nitrosomonas europaea; Oxidation-Reduction; Protein Folding; Pseudomonas aeruginosa; Recombinant Proteins; Sequence Alignment; Shewanella; Temperature; Thermodynamics	2015
Comparison of the backbone dynamics of wild-type Hydrogenobacter thermophilus cytochrome c(552) and its b-type variant. Journal of biomolecular NMR, 2015, Volume: 62, Issue:2 Topics: Alanine; Bacteria; Bacterial Proteins; Cysteine; Cytochrome c Group; Heme; Hydrogen; Models, Molecular; Nitrogen Isotopes; Nuclear Magnetic Resonance, Biomolecular; Protein Binding; Protein Conformation	2015
Replacing Arginine 33 for Alanine in the Hemophore HasA from Pseudomonas aeruginosa Causes Closure of the H32 Loop in the Apo-Protein. Biochemistry, 2016, 05-10, Volume: 55, Issue:18 Topics: Alanine; Amino Acid Substitution; Apoproteins; Arginine; Bacterial Proteins; Carrier Proteins; Heme; Iron; Molecular Dynamics Simulation; Mutation, Missense; Nuclear Magnetic Resonance, Biomolecular; Protein Structure, Secondary; Pseudomonas aeruginosa	2016
The Met80Ala and Tyr67His/Met80Ala mutants of human cytochrome c shed light on the reciprocal role of Met80 and Tyr67 in regulating ligand access into the heme pocket. Journal of inorganic biochemistry, 2017, Volume: 169 Topics: Alanine; Circular Dichroism; Cytochromes c; Heme; Histamine; Humans; Kinetics; Methionine; Models, Molecular; Mutagenesis, Site-Directed; Mutation; Protein Binding; Recombinant Proteins; Structure-Activity Relationship; Tyrosine	2017
Identification and functional analysis of new peroxygenases in oat. Planta, 2017, Volume: 246, Issue:4 Topics: Alanine; Amino Acid Sequence; Amino Acids; Avena; Binding Sites; Catalysis; Cloning, Molecular; Escherichia coli; Fatty Acids; Gene Expression; Heme; Histidine; Ligands; Mixed Function Oxygenases; Mutagenesis, Site-Directed; Mutation; Pichia; Sequence Alignment; Substrate Specificity; Transgenes	2017
The role of Ala134 in controlling substrate binding and reactivity in ascorbate peroxidase. Journal of inorganic biochemistry, 2018, Volume: 180 Topics: Alanine; Ascorbate Peroxidases; Ascorbic Acid; Catalysis; Chromatography, High Pressure Liquid; Guaiacol; Heme; Kinetics; Models, Molecular; Mutagenesis, Site-Directed; Oxidation-Reduction; Proline; Substrate Specificity	2018
Native Alanine Substitution in the Glycine Hinge Modulates Conformational Flexibility of Heme Nitric Oxide/Oxygen (H-NOX) Sensing Proteins. ACS chemical biology, 2018, 06-15, Volume: 13, Issue:6 Topics: Alanine; Bacterial Proteins; Flavobacteriaceae; Glycine; Heme; Hemeproteins; Ligands; Mutation; Nitric Oxide; Oxidation-Reduction; Pliability; Protein Binding; Protein Conformation	2018
The carboxy-terminal insert in the Q-loop is needed for functionality of Escherichia coli cytochrome bd-I. Biochimica et biophysica acta. Bioenergetics, 2020, 06-01, Volume: 1861, Issue:5-6 Topics: Alanine; Amino Acid Sequence; Cell Membrane; Cytochrome b Group; Electron Transport Chain Complex Proteins; Escherichia coli; Escherichia coli Proteins; Heme; Mutagenesis; Mutant Proteins; Oxidoreductases; Oxygen Consumption; Protein Structure, Secondary; Structure-Activity Relationship	2020
Radical Mediated Rapid Biomolecules, 2022, Sep-20, Volume: 12, Issue:10 Topics: Alanine; Cytochromes c; Escherichia coli; Heme; Manganese; Protoporphyrins; Sulfhydryl Compounds; Zinc	2022
New TSPO Crystal Structures of Mutant and Heme-Bound Forms with Altered Flexibility, Ligand Binding, and Porphyrin Degradation Activity. Biochemistry, 2023, 04-04, Volume: 62, Issue:7 Topics: Alanine; Bacterial Proteins; Binding Sites; Carrier Proteins; Heme; Ligands; Porphyrins; Protein Subunits; Rhodobacter sphaeroides	2023
An engineered thermally tolerant apo-cytochrome scaffold for metal-less incorporation of heme derivative. PloS one, 2023, Volume: 18, Issue:11 Topics: Alanine; Cytochromes c; Heme; Ligands; Methionine; Molecular Docking Simulation; Oxidation-Reduction	2023