(Q28238340)

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Structural variation in heme enzymes: a comparative analysis of peroxidase and P450 crystal structures

scientific article (publication date: 15 June 1994)

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Structural variation in heme enzymes: a comparative analysis of peroxidase and P450 crystal structures (English)

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H Li

1

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T L Poulos

series ordinal

2

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language of work or name

English

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publication date

15 June 1994

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published in

Structure

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volume

2

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issue

6

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page(s)

461-4

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cites work

Aliphatic hydroxylation by highly purified liver microsomal cytochrome P-450. Evidence for a carbon radical intermediate

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High-resolution crystal structure of cytochrome P450cam

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Crystal structure of hemoprotein domain of P450BM-3, a prototype for microsomal P450's

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7 January 2021

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Crystal structure and refinement of cytochrome P450terp at 2.3 A resolution

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The relation between the divergence of sequence and structure in proteins

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Crystal structure of substrate-free Pseudomonas putida cytochrome P-450

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A hypervariable region of P450IIC5 confers progesterone 21-hydroxylase activity to P450IIC1.

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Catalytic Sites of Hemoprotein Peroxidases

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Oxidation of monomethoxylated aromatic compounds by lignin peroxidase: role of veratryl alcohol in lignin biodegradation

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Stereochemistry and deuterium isotope effects in camphor hydroxylation by the cytochrome P450cam monoxygenase system

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Omega-1, Omega-2 and Omega-3 hydroxylation of long-chain fatty acids, amides and alcohols by a soluble enzyme system from Bacillus megaterium

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SETOR: hardware-lighted three-dimensional solid model representations of macromolecules

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Identifiers

DOI

10.1016/S0969-2126(00)00046-0

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PubMed publication ID

7922023

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(Q28238340)

Structural variation in heme enzymes: a comparative analysis of peroxidase and P450 crystal structures

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