Page last updated: 2024-08-23

heme and guanidine

heme has been researched along with guanidine in 67 studies

Research

Studies (67)

TimeframeStudies, this research(%)All Research%
pre-19903 (4.48)18.7374
1990's14 (20.90)18.2507
2000's35 (52.24)29.6817
2010's14 (20.90)24.3611
2020's1 (1.49)2.80

Authors

AuthorsStudies
Fisher, MT1
Falksen, K; Horowitz, P; Muhoberac, BB; Wharton, DC1
Bucci, E; Franchi, D; Fronticelli, C1
Bhuyan, A; Chan, CK; Eaton, WA; Henry, ER; Hofrichter, J; Hu, Y; Jones, CM; Luck, SD; Roder, H1
Chapman, SK; Coggins, JR; Daff, S; Lindsay, JG; Munro, AW1
Coggins, JR; Kelly, S; Lindsay, JG; Munro, AW; Price, NC1
Hargrove, MS; Olson, JS1
Eaton, WA; Hagen, SJ; Hofrichter, J; Szabo, A1
MacKenzie, NE; Roder, H; Sauder, JM1
Yamamoto, Y1
Chan, CK; Eaton, WA; Hofrichter, J; Hu, Y; Rousseau, DL; Takahashi, S1
Bowler, BE; Godbole, S; Hammack, B2
Dutton, PL; Gibney, BR; Rabanal, F; Reddy, KS1
Wittung-Stafshede, P1
Bocian, DF; Kalsbeck, WA; Olson, JS; Tang, Q1
Rousseau, DL; Yeh, SR1
Chattopadhyay, K; Mazumdar, S1
Eaton, WA; Hagen, SJ1
Guidry, J; Moczygemba, C; Wittung-Stafshede, P1
Ferguson, SJ; Tomlinson, EJ2
Nall, BT; Pierce, MM1
Arnesano, F; Banci, L; Bertini, I; Koulougliotis, D; Monti, A1
Bowler, BE; Nelson, CJ1
Carswell, CW; Hagen, SJ; Sjolander, EM1
Abbruzzetti, S; Libertini, LJ; Small, EW; Small, JR; Viappiani, C1
Banci, L; Bertini, I; Branchini, BR; Hajieva, P; Spyroulias, GA; Turano, P1
Bowler, BE; Hammack, BN; Smith, CR1
Bartalesi, I; Bertini, I; Ghosh, K; Rosato, A; Turano, P1
Bowler, BE; Smith, CR; Wandschneider, E1
Ascoli, F; Howes, BD; Piro, MC; Santucci, R; Sinibaldi, F; Smulevich, G1
DANIELI, G; MASETTI, GP; SANGIORGI, F1
Bowler, BE; Wandschneider, E1
Ito, A; Kudo, K; Sakamoto, S; Yoshikawa, S1
Banci, L; Barker, PD; Bruix, M; Ciofi-Baffoni, S; de Lumley Woodyear, T; Fersht, AR; Garcia, P; Johnson, CM; Ramachandra Shastry, MC; Rico, M; Roder, H1
Canters, GW; Ciofi-Baffoni, S; Diederix, RE; Lowe, CE; Prudêncio, M; Ubbink, M; Worrall, JA1
Floris, G; Longu, S; Medda, R; Mura, A; Padiglia, A; Rinaldi, AC1
Ishimori, K; Kimura, T; Morishima, I; Sakamoto, K1
Boucher, JL; Mansuy, D; Mattioli, TA; Moreau, M; Santolini, J; Stuehr, DJ1
Halder, P; Hargrove, MS; Hoy, JA; Smagghe, BJ1
Bowler, BE; Kurchan, E; Tzul, FO1
Baddam, S; Bandi, S; Bowler, BE1
Kawano, S; Tai, H; Yamamoto, Y1
Abel, CJ; Chen, E; Goldbeck, RA; Kliger, DS1
Ascenzi, P; Coletta, M; De Sanctis, G; Fanali, G; Fasano, M; Gioia, M1
Hasegawa, J; Kobayashi, Y; Nakamura, S; Sambongi, Y; Sonoyama, T; Uchiyama, S1
Munegumi, T; Tai, H; Yamamoto, Y1
Bowler, BE; Kurchan, E; Roder, H; Tzul, FO1
Gray, HB; Kimura, T; Lee, JC; Winkler, JR1
Burstyn, JN; Clark, RW; Lee, AJ; Ponter, S; Youn, H1
Li, X; Lin, Y; Mao, L; Su, L; Yu, P; Zhang, L; Zheng, W1
Balland, V; Boucher, JL; Giroud, C; Mattioli, TA; Moreau, M; Santolini, J; Stuehr, DJ; Xu-Li, Y1
Bischin, C; Cooper, CE; Damian, G; Deac, F; Rajagopal, BS; Silaghi-Dumitrescu, R; Worrall, JA1
Fuchs, MR; He, C; Knipp, M; Ogata, H1
Bandara, DM; Freeman, TL; Hong, Y; Pletneva, EV; Schiavoni, KH1
Bowler, BE; Khan, MK1
Behera, RK; Mazumdar, S; Nakajima, H; Rajbongshi, J; Watanabe, Y1
Champion, PM; Karunakaran, V; Sun, Y1
Dong, L; Jurban, BJ; Sharma, NP; Smith, WL1
Dellarole, M; Guca, E; Roumestand, C; Royer, CA; Vallone, B1
Choi, J; Fujitsuka, M; Majima, T; Tojo, S1
Barbero, L; Bojić, M; Dolgos, H; Freisleben, A; Gallemann, D; Guengerich, FP; Riva, S1
Cha, HJ; Choi, KY; Jang, DS; Jin, KS1
Olson, JS; Ou, WC; Phillips, GN; Samuel, PP1
Bowler, BE; Danielson, TA1
Ahmad, F; Ahmed, A; Hassan, MI; Islam, A; Lakhrm, NA; Malik, A; Nasreen, K; Parray, ZA; Shamsi, A1

Other Studies

67 other study(ies) available for heme and guanidine

ArticleYear
Differences in thermal stability between reduced and oxidized cytochrome b562 from Escherichia coli.
    Biochemistry, 1991, Oct-15, Volume: 30, Issue:41

    Topics: Cytochrome b Group; Electron Transport; Enzyme Stability; Escherichia coli; Escherichia coli Proteins; Guanidine; Guanidines; Heme; Kinetics; Oxidation-Reduction; Protein Conformation; Protein Denaturation; Spectrophotometry, Ultraviolet; Thermodynamics

1991
Perturbation of Pseudomonas cytochrome oxidase by guanidine hydrochloride to detect differential stabilization of the heme d1 and heme c moieties.
    Biochimica et biophysica acta, 1986, Jun-05, Volume: 871, Issue:2

    Topics: Chromatography, Gel; Circular Dichroism; Electron Transport Complex IV; Guanidine; Guanidines; Heme; Macromolecular Substances; Pseudomonas; Spectrometry, Fluorescence

1986
Folding domains as functional tools in allosteric systems: a heme-dependent domain in hemoglobin beta subunits.
    Biochemistry, 1982, Nov-23, Volume: 21, Issue:24

    Topics: Allosteric Site; Guanidine; Guanidines; Heme; Hemoglobins; Hydrogen-Ion Concentration; Kinetics; Macromolecular Substances; Mathematics; Protein Conformation; Temperature; Thermodynamics

1982
Fast events in protein folding initiated by nanosecond laser photolysis.
    Proceedings of the National Academy of Sciences of the United States of America, 1993, Dec-15, Volume: 90, Issue:24

    Topics: Amino Acid Sequence; Animals; Binding Sites; Carbon Monoxide; Cytochrome c Group; Guanidine; Guanidines; Heme; Horses; Kinetics; Lasers; Methionine; Photolysis; Protein Conformation; Protein Folding; Protein Structure, Secondary; Spectrophotometry; Time Factors

1993
Formation of flavin semiquinone during the reduction of P450 BM3 reductase domain with NADPH.
    Biochemical Society transactions, 1996, Volume: 24, Issue:1

    Topics: Bacillus megaterium; Bacterial Proteins; Cytochrome P-450 Enzyme System; Flavin Mononucleotide; Flavin-Adenine Dinucleotide; Guanidine; Guanidines; Heme; Kinetics; Mixed Function Oxygenases; NAD; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Quinones; Spectrophotometry

1996
Deflavination of cytochrome P450 BM3 by treatment with guanidinium chloride.
    Biochemical Society transactions, 1996, Volume: 24, Issue:1

    Topics: Bacillus megaterium; Bacterial Proteins; Circular Dichroism; Cytochrome P-450 Enzyme System; Flavins; Guanidine; Guanidines; Heme; Mixed Function Oxygenases; NADPH-Ferrihemoprotein Reductase; Oxidation-Reduction; Protein Conformation

1996
The stability of holomyoglobin is determined by heme affinity.
    Biochemistry, 1996, Sep-03, Volume: 35, Issue:35

    Topics: Animals; Binding Sites; Circular Dichroism; Fluorescence; Globins; Guanidine; Guanidines; Heme; Iron; Kinetics; Metmyoglobin; Mutagenesis; Myoglobin; Oxidation-Reduction; Protein Binding; Protein Denaturation; Protein Folding; Recombinant Proteins; Spectrophotometry; Whales

1996
Diffusion-limited contact formation in unfolded cytochrome c: estimating the maximum rate of protein folding.
    Proceedings of the National Academy of Sciences of the United States of America, 1996, Oct-15, Volume: 93, Issue:21

    Topics: Cytochrome c Group; Diffusion; Guanidine; Guanidines; Heme; Kinetics; Ligands; Methionine; Models, Structural; Peroxidases; Protein Conformation; Protein Denaturation; Protein Folding; Spectrophotometry; Time Factors

1996
Kinetic mechanism of folding and unfolding of Rhodobacter capsulatus cytochrome c2.
    Biochemistry, 1996, Dec-24, Volume: 35, Issue:51

    Topics: Cytochrome c Group; Cytochromes c2; Guanidine; Guanidines; Heme; Kinetics; Models, Molecular; Protein Conformation; Protein Denaturation; Protein Folding; Rhodobacter capsulatus; Solvents; Thermodynamics

1996
1H-NMR study of inter-segmental hydrogen bonds in sperm whale and horse apomyoglobins.
    European journal of biochemistry, 1997, Jan-15, Volume: 243, Issue:1-2

    Topics: Animals; Apoproteins; Aspartic Acid; Guanidine; Guanidines; Heme; Histidine; Horses; Hydrogen Bonding; Hydrogen-Ion Concentration; Magnetic Resonance Spectroscopy; Myoglobin; Protein Conformation; Protein Denaturation; Temperature; Whales

1997
Submillisecond protein folding kinetics studied by ultrarapid mixing.
    Proceedings of the National Academy of Sciences of the United States of America, 1997, Mar-04, Volume: 94, Issue:5

    Topics: Animals; Cytochrome c Group; Fluorescence; Guanidine; Guanidines; Heme; Horses; Imidazoles; Kinetics; Myocardium; Protein Denaturation; Protein Folding; Tryptophan

1997
Cytochrome c folding traps are not due solely to histidine-heme ligation: direct demonstration of a role for N-terminal amino group-heme ligation.
    Journal of molecular biology, 1998, Feb-06, Volume: 275, Issue:5

    Topics: Cytochrome c Group; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Protein Denaturation; Protein Folding

1998
Effect of four helix bundle topology on heme binding and redox properties.
    Biochemistry, 1998, Mar-31, Volume: 37, Issue:13

    Topics: Amino Acid Sequence; Carbon Monoxide; Chromatography, Gel; Circular Dichroism; Guanidine; Heme; Hemeproteins; Iron Compounds; Ligands; Molecular Sequence Data; Oxidation-Reduction; Peptides; Protein Binding; Protein Denaturation; Protein Structure, Secondary

1998
A stable, molten-globule-like cytochrome c.
    Biochimica et biophysica acta, 1998, Feb-17, Volume: 1382, Issue:2

    Topics: Circular Dichroism; Cytochrome c Group; Escherichia coli; Guanidine; Heme; Oxidation-Reduction; Protein Denaturation; Protein Folding; Recombinant Proteins; Sequence Analysis; Thermus thermophilus; Tryptophan

1998
Disruption of the heme iron-proximal histidine bond requires unfolding of deoxymyoglobin.
    Biochemistry, 1998, May-12, Volume: 37, Issue:19

    Topics: Acids; Animals; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Iron; Kinetics; Male; Mutagenesis, Site-Directed; Myoglobin; Protein Folding; Spectrophotometry; Spermatozoa; Whales

1998
Ligand exchange during unfolding of cytochrome c.
    The Journal of biological chemistry, 1999, Jun-18, Volume: 274, Issue:25

    Topics: Animals; Circular Dichroism; Cytochrome c Group; Guanidine; Heme; Horses; Kinetics; Ligands; Myocardium; Protein Denaturation; Protein Folding; Scattering, Radiation; Spectrometry, Fluorescence; Thermodynamics; Tryptophan

1999
Structural and conformational stability of horseradish peroxidase: effect of temperature and pH.
    Biochemistry, 2000, Jan-11, Volume: 39, Issue:1

    Topics: Calcium; Circular Dichroism; Enzyme Stability; Guanidine; Heme; Horseradish Peroxidase; Hydrogen-Ion Concentration; Models, Molecular; Protein Conformation; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Spectrometry, Fluorescence; Temperature; Tryptophan

2000
Measuring denatured state energetics: deviations from random coil behavior and implications for the folding of iso-1-cytochrome c.
    Journal of molecular biology, 2000, Feb-11, Volume: 296, Issue:1

    Topics: Binding, Competitive; Biopolymers; Circular Dichroism; Cytochrome c Group; Cytochromes c; Enzyme Stability; Genetic Variation; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Kinetics; Ligands; Models, Chemical; Protein Conformation; Protein Denaturation; Protein Folding; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Thermodynamics; Titrimetry

2000
Two-state expansion and collapse of a polypeptide.
    Journal of molecular biology, 2000, Mar-31, Volume: 297, Issue:3

    Topics: Animals; Computer Simulation; Cytochrome c Group; Diffusion; Guanidine; Heme; Horses; Kinetics; Lasers; Models, Chemical; Peptides; Protein Conformation; Protein Denaturation; Protein Folding; Solvents; Spectrometry, Fluorescence; Temperature; Thermodynamics; Tryptophan; Viscosity

2000
Heme orientation affects holo-myoglobin folding and unfolding kinetics.
    FEBS letters, 2000, Mar-24, Volume: 470, Issue:2

    Topics: Animals; Apoproteins; Circular Dichroism; Dose-Response Relationship, Drug; Fluorescence; Guanidine; Heme; Horses; Kinetics; Metmyoglobin; Myoglobin; Protein Denaturation; Protein Folding; Protein Renaturation; Rotation; Thermodynamics; Tryptophan; Whales

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
Coupled kinetic traps in cytochrome c folding: His-heme misligation and proline isomerization.
    Journal of molecular biology, 2000, May-19, Volume: 298, Issue:5

    Topics: Amino Acid Sequence; Amino Acid Substitution; Binding Sites; Cytochrome c Group; Cytochromes c; Enzyme Stability; Fluorescence; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Isomerism; Kinetics; Models, Molecular; Molecular Sequence Data; Mutation; Proline; Protein Conformation; Protein Denaturation; Protein Folding; Protein Renaturation; Saccharomyces cerevisiae; Sequence Alignment; Thermodynamics

2000
Monitoring mobility in the early steps of unfolding: the case of oxidized cytochrome b(5) in the presence of 2 M guanidinium chloride.
    Biochemistry, 2000, Jun-20, Volume: 39, Issue:24

    Topics: Animals; Cytochromes b5; Guanidine; Heme; Kinetics; Magnetic Resonance Spectroscopy; Microsomes; Models, Molecular; Nitrogen Isotopes; Protein Conformation; Protein Denaturation; Protein Folding; Rats

2000
Loss of either of the two heme-binding cysteines from a class I c-type cytochrome has a surprisingly small effect on physicochemical properties.
    The Journal of biological chemistry, 2000, Oct-20, Volume: 275, Issue:42

    Topics: Amino Acid Sequence; Amino Acid Substitution; Bacteria, Aerobic; Base Sequence; Binding Sites; Cloning, Molecular; Cysteine; Cytochrome c Group; Escherichia coli; Guanidine; Heme; Kinetics; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Protein Denaturation; Protein Folding; Recombinant Proteins; Templates, Genetic

2000
pH dependence of formation of a partially unfolded state of a Lys 73 --> His variant of iso-1-cytochrome c: implications for the alkaline conformational transition of cytochrome c.
    Biochemistry, 2000, Nov-07, Volume: 39, Issue:44

    Topics: Amino Acid Substitution; Cytochrome c Group; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Isoenzymes; Lysine; Models, Chemical; Mutagenesis, Site-Directed; Nuclear Magnetic Resonance, Biomolecular; Protein Conformation; Protein Folding; Saccharomyces cerevisiae; Titrimetry

2000
Rate of intrachain contact formation in an unfolded protein: temperature and denaturant effects.
    Journal of molecular biology, 2001, Feb-02, Volume: 305, Issue:5

    Topics: Animals; Binding Sites; Cytochrome c Group; Diffusion; Dose-Response Relationship, Drug; Guanidine; Heme; Horses; Kinetics; Ligands; Methionine; Protein Conformation; Protein Denaturation; Protein Folding; Solvents; Temperature; Thermodynamics

2001
Kinetics of histidine deligation from the heme in GuHCl-unfolded Fe(III) cytochrome C studied by a laser-induced pH-jump technique.
    Journal of the American Chemical Society, 2001, Jul-11, Volume: 123, Issue:27

    Topics: Animals; Bacterial Proteins; Cytochrome c Group; Guanidine; Heme; Histidine; Horses; Hydrogen-Ion Concentration; Kinetics; Lasers; Ligands; Protein Folding

2001
Dimethyl propionate ester heme-containing cytochrome b5: structure and stability.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2001, Volume: 6, Issue:5-6

    Topics: Amino Acid Sequence; Cytochromes b5; Enzyme Stability; Guanidine; Heme; Magnetic Resonance Spectroscopy; Magnetics; Metalloporphyrins; Molecular Sequence Data; Protein Conformation; Protein Folding

2001
Denatured state thermodynamics: residual structure, chain stiffness and scaling factors.
    Journal of molecular biology, 2001, Aug-31, Volume: 311, Issue:5

    Topics: Acetylation; Circular Dichroism; Cytochrome c Group; Cytochromes c; Enzyme Stability; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Mutation; Protein Binding; Protein Conformation; Protein Denaturation; Protein Folding; Saccharomyces cerevisiae Proteins; Serine Endopeptidases; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Thermodynamics; Titrimetry; Yeasts

2001
The unfolding of oxidized c-type cytochromes: the instructive case of Bacillus pasteurii.
    Journal of molecular biology, 2002, Aug-23, Volume: 321, Issue:4

    Topics: Bacillus; Cytochrome c Group; Guanidine; Heme; Hydrogen-Ion Concentration; Iron; Ligands; Magnetic Resonance Spectroscopy; Methionine; Mitochondria; Models, Molecular; Oxidation-Reduction; Protein Conformation; Protein Denaturation; Protein Folding; Spectrum Analysis; Thermodynamics

2002
Effect of pH on the iso-1-cytochrome c denatured state: changing constraints due to heme ligation.
    Biochemistry, 2003, Feb-25, Volume: 42, Issue:7

    Topics: Acetylation; Amino Acid Substitution; Binding, Competitive; Cytochrome c Group; Cytochromes c; Genetic Variation; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Ligands; Lysine; Mutagenesis, Site-Directed; Protein Conformation; Protein Denaturation; Protein Structure, Tertiary; Saccharomyces cerevisiae Proteins; Spectrometry, Fluorescence; Tryptophan

2003
Rupture of the hydrogen bond linking two Omega-loops induces the molten globule state at neutral pH in cytochrome c.
    Biochemistry, 2003, Jun-24, Volume: 42, Issue:24

    Topics: Amino Acid Substitution; Circular Dichroism; Cytochrome c Group; Electrochemistry; Guanidine; Heme; Hydrogen Bonding; Hydrogen-Ion Concentration; Models, Molecular; Mutagenesis, Site-Directed; Protein Denaturation; Protein Folding; Recombinant Proteins; Spectrophotometry; Spectrum Analysis, Raman; Thermodynamics; Yeasts

2003
[Action of various aromatic substances and nitrogen metabolites on heme synthesis in vitro].
    Bollettino della Societa italiana di biologia sperimentale, 1963, Mar-15, Volume: 39

    Topics: Creatine; Creatinine; Guanidine; Guanidines; Heme; In Vitro Techniques; Indoles; Nitrogen; Phenols; Urea; Uric Acid

1963
Conformational properties of the iso-1-cytochrome C denatured state: dependence on guanidine hydrochloride concentration.
    Journal of molecular biology, 2004, May-21, Volume: 339, Issue:1

    Topics: Cytochromes c; Guanidine; Heme; Histidine; Isoenzymes; Protein Conformation; Protein Denaturation; Protein Folding; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins

2004
De novo design, synthesis, and function of semiartificial myoglobin conjugated with coiled-coil two-alpha-helix peptides.
    Chemistry (Weinheim an der Bergstrasse, Germany), 2004, Aug-06, Volume: 10, Issue:15

    Topics: Amino Acid Sequence; Chromatography, High Pressure Liquid; Flavins; Guanidine; Heme; Models, Molecular; Molecular Sequence Data; Myoglobin; NAD; Peptides; Protein Conformation; Protein Denaturation; Protein Structure, Secondary; Spectrometry, Fluorescence; Structure-Activity Relationship

2004
Effects of heme on the structure of the denatured state and folding kinetics of cytochrome b562.
    Journal of molecular biology, 2005, Feb-11, Volume: 346, Issue:1

    Topics: Amino Acid Sequence; Apoproteins; Circular Dichroism; Cytochrome b Group; Escherichia coli; Escherichia coli Proteins; Guanidine; Heme; Hydrogen-Ion Concentration; Kinetics; Models, Molecular; Molecular Sequence Data; Mutation; Nuclear Magnetic Resonance, Biomolecular; Protein Denaturation; Protein Folding; Protein Structure, Tertiary; Thermodynamics; Tryptophan; Urea

2005
The effects of ligand exchange and mobility on the peroxidase activity of a bacterial cytochrome c upon unfolding.
    Chembiochem : a European journal of chemical biology, 2005, Volume: 6, Issue:4

    Topics: Amino Acid Substitution; Cytochrome c Group; Guanidine; Heme; Hydrogen-Ion Concentration; Kinetics; Magnetic Resonance Spectroscopy; Paracoccus; Peroxidase; Protein Conformation; Protein Denaturation; Protein Folding; Spectrophotometry; Spectrophotometry, Ultraviolet; Thermodynamics

2005
Reversible thermal inactivation and conformational states in denaturant guanidinium of a calcium-dependent peroxidase from Euphorbia characias.
    International journal of biological macromolecules, 2005, Dec-15, Volume: 37, Issue:4

    Topics: Calcium; Enzyme Activation; Enzyme Stability; Euphorbia; Guanidine; Heme; Kinetics; Peroxidase; Plant Proteins; Protein Conformation; Protein Denaturation; Temperature

2005
Dehydration in the folding of reduced cytochrome c revealed by the electron-transfer-triggered folding under high pressure.
    Journal of the American Chemical Society, 2006, Jan-25, Volume: 128, Issue:3

    Topics: Cytochromes c; Guanidine; Heme; Hydrophobic and Hydrophilic Interactions; Kinetics; Oxidation-Reduction; Pressure; Protein Folding; Water

2006
Differential effects of alkyl- and arylguanidines on the stability and reactivity of inducible NOS heme-dioxygen complexes.
    Biochemistry, 2006, Mar-28, Volume: 45, Issue:12

    Topics: Animals; Carbon Monoxide; Enzyme Stability; Guanidine; Heme; Mice; Nitric Oxide Synthase Type II; Oxygen; Spectroscopy, Fourier Transform Infrared; Spectrum Analysis, Raman

2006
Covalent heme attachment in Synechocystis hemoglobin is required to prevent ferrous heme dissociation.
    Protein science : a publication of the Protein Society, 2007, Volume: 16, Issue:2

    Topics: Binding Sites; Carbon Monoxide; Crystallography, X-Ray; Cyanides; Guanidine; Heme; Hemoglobins; Histidine; Iron; Ligands; Protein Binding; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Synechocystis

2007
Sequence composition effects on denatured state loop formation in iso-1-cytochrome c variants: polyalanine versus polyglycine inserts.
    Journal of molecular biology, 2007, Aug-17, Volume: 371, Issue:3

    Topics: Amino Acid Sequence; Cytochromes c; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Molecular Sequence Data; Mutagenesis, Insertional; Mutant Proteins; Peptides; Protein Denaturation; Protein Structure, Secondary; Saccharomyces cerevisiae Proteins; Thermodynamics; Titrimetry

2007
Alkaline conformational transition and gated electron transfer with a Lys 79 --> his variant of iso-1-cytochrome c.
    Biochemistry, 2007, Sep-18, Volume: 46, Issue:37

    Topics: Alkalies; Anaerobiosis; Cytochromes c; Electron Transport; Guanidine; Heme; Histidine; Hydrogen-Ion Concentration; Kinetics; Ligands; Lysine; Magnetic Resonance Spectroscopy; Mutant Proteins; Protein Conformation; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Protons; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Thermodynamics

2007
Characterization of N-terminal amino group-heme ligation emerging upon guanidine hydrochloric acid induced unfolding of Hydrogenobacter thermophilus ferricytochrome c552.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2008, Volume: 13, Issue:1

    Topics: Acids; Bacteria; Circular Dichroism; Cytochromes c; Guanidine; Heme; Hydrogen-Ion Concentration; Nuclear Magnetic Resonance, Biomolecular; Protein Denaturation; Spectrophotometry, Ultraviolet

2008
Non-native heme-histidine ligation promotes microsecond time scale secondary structure formation in reduced horse heart cytochrome c.
    Biochemistry, 2007, Oct-30, Volume: 46, Issue:43

    Topics: Animals; Circular Dichroism; Cytochromes c; Guanidine; Heme; Histidine; Horses; Myocardium; Protein Folding; Protein Structure, Secondary; Spectrophotometry, Ultraviolet

2007
Reversible two-step unfolding of heme-human serum albumin: a (1)H-NMR relaxometric and circular dichroism study.
    Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2009, Volume: 14, Issue:2

    Topics: Binding Sites; Circular Dichroism; Guanidine; Heme; Humans; Magnetic Resonance Spectroscopy; Models, Molecular; Myristic Acid; Protein Conformation; Protein Denaturation; Protein Folding; Protons; Serum Albumin

2009
Stability enhancement of cytochrome c through heme deprotonation and mutations.
    Biophysical chemistry, 2009, Volume: 139, Issue:1

    Topics: Bacterial Proteins; Cytochromes c; Guanidine; Heme; Hydrogen Bonding; Hydrogen-Ion Concentration; Mutation; Protein Denaturation; Protein Stability; Protons; Pseudomonas aeruginosa

2009
Stability of the heme Fe-N-terminal amino group coordination bond in denatured cytochrome c.
    Inorganic chemistry, 2009, Jan-05, Volume: 48, Issue:1

    Topics: Amino Acid Sequence; Aquifoliaceae; Cytochromes c; Electrons; Guanidine; Heme; Histidine; Iron; Magnetic Resonance Spectroscopy; Mutation; Nitrogen; Oxidation-Reduction; Protein Denaturation; Pseudomonas aeruginosa

2009
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
Folding energy landscape of cytochrome cb562.
    Proceedings of the National Academy of Sciences of the United States of America, 2009, May-12, Volume: 106, Issue:19

    Topics: Biochemistry; Cytochrome b Group; Databases, Protein; Escherichia coli; Escherichia coli Proteins; Fluorescence Resonance Energy Transfer; Guanidine; Heme; Kinetics; Models, Statistical; Molecular Conformation; Protein Conformation; Protein Denaturation; Protein Folding; Protein Structure, Secondary

2009
Guanidine hydrochloride-induced unfolding of the three heme coordination states of the CO-sensing transcription factor, CooA.
    Biochemistry, 2009, Jul-21, Volume: 48, Issue:28

    Topics: Bacterial Proteins; Biosensing Techniques; Carbon Monoxide; Circular Dichroism; DNA; Guanidine; Heme; Hemeproteins; Iron; Models, Molecular; Mutant Proteins; Protein Binding; Protein Denaturation; Protein Folding; Protein Structure, Secondary; Protein Structure, Tertiary; Spectrometry, Fluorescence; Thermodynamics; Trans-Activators; Transcription Factors

2009
Effective electrochemical method for investigation of hemoglobin unfolding based on the redox property of heme groups at glassy carbon electrodes.
    Analytical chemistry, 2009, Oct-15, Volume: 81, Issue:20

    Topics: Animals; Carbon; Catalase; Catalytic Domain; Cattle; Electrochemistry; Electrodes; Glass; Guanidine; Heme; Hemoglobins; Hydrogen-Ion Concentration; Hydrophobic and Hydrophilic Interactions; Models, Molecular; Oxidation-Reduction; Peptides; Protein Denaturation; Protein Renaturation; Protein Subunits; Spectrum Analysis

2009
Role of arginine guanidinium moiety in nitric-oxide synthase mechanism of oxygen activation.
    The Journal of biological chemistry, 2010, Mar-05, Volume: 285, Issue:10

    Topics: Animals; Arginine; Binding Sites; Catalytic Domain; Citrulline; Enzyme Activation; Guanidine; Heme; Hydrogen Bonding; Mice; Models, Molecular; Molecular Structure; Nitric Oxide; Nitric Oxide Synthase Type II; Oxidation-Reduction; Oxygen; Reactive Nitrogen Species; Reactive Oxygen Species; Spectroscopy, Fourier Transform Infrared; Spectrum Analysis, Raman

2010
Ascorbate peroxidase activity of cytochrome c.
    Free radical research, 2011, Volume: 45, Issue:4

    Topics: Animals; Apoptosis; Ascorbic Acid; Cardiolipins; Cattle; Cytochrome-c Peroxidase; Cytochromes c; Free Radicals; Guanidine; Heme; Horses; Hydrogen Peroxide; Iron; Kinetics; Methylation; Mitochondria, Heart; Signal Transduction; Spectrum Analysis; Yeasts

2011
Guanidine-ferroheme coordination in the mutant protein nitrophorin 4(L130R).
    Angewandte Chemie (International ed. in English), 2012, Apr-27, Volume: 51, Issue:18

    Topics: Guanidine; Heme; Hemeproteins; Mutant Proteins; Organometallic Compounds; Salivary Proteins and Peptides; Water

2012
Changes in the heme ligation during folding of a Geobacter sulfurreducens sensor GSU0935.
    Dalton transactions (Cambridge, England : 2003), 2012, Jul-14, Volume: 41, Issue:26

    Topics: Amino Acid Substitution; Cytochrome c Group; Geobacter; Guanidine; Heme; Hydrogen-Ion Concentration; Kinetics; Ligands; Oxidation-Reduction; Protein Refolding; Protein Structure, Tertiary; Water

2012
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
Thermodynamic effects of the alteration of the axial ligand on the unfolding of thermostable cytochrome C.
    Biochemistry, 2013, Feb-26, Volume: 52, Issue:8

    Topics: Catalytic Domain; Circular Dichroism; Cytochrome c Group; Electrochemical Techniques; Guanidine; Heme; Models, Molecular; Mutagenesis, Site-Directed; Point Mutation; Protein Conformation; Protein Stability; Protein Unfolding; Spectrophotometry, Ultraviolet; Temperature; Thermodynamics; Thermus thermophilus

2013
Investigations of the low-frequency spectral density of cytochrome c upon equilibrium unfolding.
    The journal of physical chemistry. B, 2013, Aug-22, Volume: 117, Issue:33

    Topics: Animals; Cytochromes c; Guanidine; Heme; Horses; Hydrogen-Ion Concentration; Models, Molecular; Protein Denaturation; Spectrophotometry, Ultraviolet; Spectrum Analysis, Raman; Temperature; Thermodynamics

2013
Pre-existent asymmetry in the human cyclooxygenase-2 sequence homodimer.
    The Journal of biological chemistry, 2013, Oct-04, Volume: 288, Issue:40

    Topics: Acetylation; Amino Acid Sequence; Amino Acid Substitution; Anti-Inflammatory Agents, Non-Steroidal; Arachidonic Acid; Aspirin; Celecoxib; Cyclooxygenase 2; Cyclooxygenase Inhibitors; Flurbiprofen; Guanidine; Heme; Humans; Indomethacin; Kinetics; Models, Biological; Mutant Proteins; Mutation; Naproxen; Oxygen; Palmitic Acid; Peroxidase; Protein Multimerization; Pyrazoles; Substrate Specificity; Sulfonamides

2013
Low-cost equilibrium unfolding of heme proteins using 2 μl samples.
    Analytical biochemistry, 2013, Dec-01, Volume: 443, Issue:1

    Topics: Bacterial Proteins; Binding Sites; Circular Dichroism; Cytochromes b5; Globins; Guanidine; Heme; Kinetics; Nerve Tissue Proteins; Neuroglobin; Protein Denaturation; Protein Folding; Protein Stability; Protein Unfolding; Spectrometry, Fluorescence; Structure-Activity Relationship; Thermodynamics; Truncated Hemoglobins

2013
Dynamics in the heme geometry of myoglobin induced by the one-electron reduction.
    International journal of radiation biology, 2014, Volume: 90, Issue:6

    Topics: Animals; Electrons; Guanidine; Heme; Horses; Metmyoglobin; Models, Molecular; Myoglobin; Oxidation-Reduction; Protein Conformation; Protein Folding; Pulse Radiolysis; Spectrum Analysis, Raman

2014
Time- and NADPH-dependent inhibition of cytochrome P450 3A4 by the cyclopentapeptide cilengitide: significance of the guanidine group and accompanying spectral changes.
    Drug metabolism and disposition: the biological fate of chemicals, 2014, Volume: 42, Issue:9

    Topics: Adult; Cytochrome P-450 CYP3A; Enzyme Inhibitors; Female; Guanidine; Heme; Humans; Male; Microsomes, Liver; NADP; Oxidation-Reduction; Snake Venoms

2014
Structural analyses combined with small-angle X-ray scattering reveals that the retention of heme is critical for maintaining the structure of horseradish peroxidase under denaturing conditions.
    Amino acids, 2017, Volume: 49, Issue:4

    Topics: Circular Dichroism; Guanidine; Heme; Horseradish Peroxidase; Models, Molecular; Protein Denaturation; Protein Structure, Tertiary; Protein Unfolding; Temperature; Urea; X-Ray Diffraction

2017
Mechanism of Human Apohemoglobin Unfolding.
    Biochemistry, 2017, 03-14, Volume: 56, Issue:10

    Topics: Apoproteins; Cloning, Molecular; Escherichia coli; Fetal Hemoglobin; Gene Expression; Glycine; Guanidine; Heme; Hemoglobin A; Hemoglobins; Humans; Kinetics; Protein Denaturation; Protein Domains; Protein Folding; Protein Multimerization; Protein Stability; Protein Structure, Secondary; Protein Unfolding; Recombinant Proteins

2017
Helical Propensity Affects the Conformational Properties of the Denatured State of Cytochrome c'.
    Biophysical journal, 2018, 01-23, Volume: 114, Issue:2

    Topics: Cytochromes c; Guanidine; Heme; Kinetics; Models, Molecular; Mutagenesis; Protein Conformation, alpha-Helical; Protein Denaturation; Rhodopseudomonas

2018
Crowding Milleu stabilizes apo-myoglobin against chemical-induced denaturation: Dominance of hardcore repulsions in the heme devoid protein.
    International journal of biological macromolecules, 2021, Jun-30, Volume: 181

    Topics: Animals; Apoproteins; Dextrans; Ficoll; Guanidine; Heme; Horses; Macromolecular Substances; Myoglobin; Protein Conformation; Protein Denaturation; Protein Stability; Spectrophotometry, Ultraviolet; Thermodynamics; Urea

2021
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