Page last updated: 2024-08-23

heme and fusarium

heme has been researched along with fusarium in 8 studies

Research

Studies (8)

TimeframeStudies, this research(%)All Research%
pre-19901 (12.50)18.7374
1990's4 (50.00)18.2507
2000's3 (37.50)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Fukamizu, A; Gotoh, O; Hoshino, T; Kizawa, H; Oda, M; Shoun, H; Tomura, D; Yasui, T1
Emery, T1
Imai, Y; Nakahara, K; Okamoto, N; Shoun, H1
Adachi, S; Hori, H; Iizuka, T; Nakagawa, A; Park, SY; Shimizu, H; Shiro, Y; Shoun, H; Tanaka, I1
Adachi, S; Iizuka, T; Nakagawa, A; Nakahara, K; Nakamura, H; Obayashi, E; Park, SY; Shimizu, H; Shiro, Y; Shoun, H; Tanaka, I1
Adachi, S; Arakawa, H; Gomi, Y; Nakamura, H; Obayashi, E; Park, SY; Shimizu, H; Shiro, Y; Shoun, H1
Lee, D; Park, S; Shimizu, H; Shiro, Y; Shoun, H1
Fushinobu, S; Shoun, H; Su, F; Takaya, N1

Reviews

1 review(s) available for heme and fusarium

ArticleYear
Hydroxamic acids of natural origin.
    Advances in enzymology and related areas of molecular biology, 1971, Volume: 35

    Topics: Actinomyces; Anti-Bacterial Agents; Aspergillus; Basidiomycota; Binding Sites; Biological Transport; Candida; Fusarium; Heme; Hydroxamic Acids; Iron; Molecular Conformation; Mycobacterium; Oligopeptides; Oxidation-Reduction; Penicillium; Periodic Acid; Streptomyces

1971

Other Studies

7 other study(ies) available for heme and fusarium

ArticleYear
Nucleotide sequence of the unique nitrate/nitrite-inducible cytochrome P-450 cDNA from Fusarium oxysporum.
    The Journal of biological chemistry, 1991, Jun-05, Volume: 266, Issue:16

    Topics: Amino Acid Sequence; Base Sequence; Biological Evolution; Cytochrome P-450 Enzyme System; DNA; Fusarium; Heme; Molecular Sequence Data; Nitrates; Nitrites; Restriction Mapping; Sequence Alignment; Sequence Homology, Nucleic Acid

1991
Absorption spectral studies on heme ligand interactions of P-450nor.
    Biochimica et biophysica acta, 1997, Jan-04, Volume: 1337, Issue:1

    Topics: Binding, Competitive; Camphor 5-Monooxygenase; Carbon Monoxide; Cytochrome P-450 Enzyme System; Ferric Compounds; Ferrous Compounds; Fusarium; Heme; Imidazoles; Ligands; Nitriles; Oxidoreductases; Pyridines; Spectrophotometry; Titrimetry

1997
Crystallization, preliminary diffraction and electron paramagnetic resonance studies of a single crystal of cytochrome P450nor.
    FEBS letters, 1997, Jul-28, Volume: 412, Issue:2

    Topics: Crystallography, X-Ray; Cytochrome P-450 Enzyme System; Electron Spin Resonance Spectroscopy; Fusarium; Heme; Iron; Oxidoreductases; Protein Conformation

1997
Crystal structure of nitric oxide reductase from denitrifying fungus Fusarium oxysporum.
    Nature structural biology, 1997, Volume: 4, Issue:10

    Topics: Amino Acid Sequence; Binding Sites; Carbon Monoxide; Crystallography, X-Ray; Fusarium; Heme; Iron; Models, Structural; Molecular Sequence Data; NAD; Oxidoreductases; Protein Conformation; Protein Structure, Secondary; Recombinant Proteins; Solvents

1997
Proton delivery in NO reduction by fungal nitric-oxide reductase. Cryogenic crystallography, spectroscopy, and kinetics of ferric-NO complexes of wild-type and mutant enzymes.
    The Journal of biological chemistry, 2000, Feb-18, Volume: 275, Issue:7

    Topics: Aspartic Acid; Base Sequence; Catalysis; Crystallography, X-Ray; DNA Primers; Ferric Compounds; Fusarium; Heme; Hydrogen Bonding; Kinetics; Models, Molecular; Molecular Structure; Mutagenesis, Site-Directed; Nitric Oxide; Oxidation-Reduction; Oxidoreductases; Protons; Serine

2000
Crystal structures of cytochrome P450nor and its mutants (Ser286-->Val, Thr) in the ferric resting state at cryogenic temperature: a comparative analysis with monooxygenase cytochrome P450s.
    Journal of inorganic biochemistry, 2000, Aug-31, Volume: 81, Issue:3

    Topics: Binding Sites; Crystallography, X-Ray; Cytochrome P-450 Enzyme System; Electrons; Fusarium; Heme; Hydrogen Bonding; Kinetics; Ligands; Models, Molecular; Mutation; Nitric Oxide; Oxidoreductases; Protein Conformation; Protein Structure, Secondary; Protons; Recombinant Proteins; Serine; Spectrophotometry; Temperature; Threonine; Valine; Water

2000
Involvement of a Glu71-Arg64 couple in the access channel for NADH in cytochrome p450nor.
    Bioscience, biotechnology, and biochemistry, 2004, Volume: 68, Issue:5

    Topics: Amino Acid Substitution; Arginine; Aspartic Acid; Cytochrome P-450 Enzyme System; Fusarium; Glutamic Acid; Heme; Molecular Structure; NAD; Oxidoreductases; Point Mutation

2004