Abstract
Putative access channel for NADH in the heme-distal pocket of cytochrome p450nor (p450nor) comprises many charged amino acid residues. Characterization of the E71A mutant protein of p450nor highlights the existence of a unique mechanism for binding NADH that depends on the salt bridge network between Glu71, Arg64 and Asp88.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Substitution / genetics
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Arginine / chemistry
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Aspartic Acid / chemistry
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Cytochrome P-450 Enzyme System / chemistry*
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Cytochrome P-450 Enzyme System / genetics*
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Fusarium / enzymology
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Glutamic Acid / chemistry
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Heme / chemistry
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Molecular Structure
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NAD / chemistry*
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Oxidoreductases / chemistry*
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Oxidoreductases / genetics*
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Point Mutation
Substances
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NAD
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Aspartic Acid
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Glutamic Acid
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Heme
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Cytochrome P-450 Enzyme System
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Arginine
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Oxidoreductases
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nitric-oxide reductase (P450)