Mutation effects of a conserved threonine (Thr243) of cytochrome P450nor on its structure and function (Q27629045)

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H Shimizu

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S Y Park

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H Shoun

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Y Shiro

Journal of Inorganic Biochemistry

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publication date

November 2000

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published in

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volume

82

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issue

1-4

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page(s)

103-11

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cites work

Purification and properties of a cytochrome P-450 of a fungus, Fusarium oxysporum

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Crystal structure of nitric oxide reductase from denitrifying fungus Fusarium oxysporum

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Spectroscopic and kinetic studies on reaction of cytochrome P450nor with nitric oxide. Implication for its nitric oxide reduction mechanism

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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

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Site-directed mutagenesis of the conserved threonine (Thr243) of the distal helix of fungal cytochrome P450nor

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Uncoupling of the cytochrome P-450cam monooxygenase reaction by a single mutation, threonine-252 to alanine or valine: possible role of the hydroxy amino acid in oxygen activation

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Crystal structure of the cytochrome P-450CAM active site mutant Thr252Ala

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Role of Thr-252 in cytochrome P450cam: a study with unnatural amino acid mutagenesis

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Understanding the role of the essential Asp251 in cytochrome p450cam using site-directed mutagenesis, crystallography, and kinetic solvent isotope effect

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The catalytic pathway of cytochrome p450cam at atomic resolution

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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

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The effects of heme modification on reactivity, ligand binding properties and iron-coordination structures of cytochrome P450nor

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Functional and structural comparison of nitric oxide reductases from denitrifying fungi Cylindrocarpon tonkinense and Fusarium oxysporum

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