MauG, a diheme enzyme that catalyzes tryptophan tryptophylquinone biosynthesis by remote catalysis.
about
A T67A mutation in the proximal pocket of the high-spin heme of MauG stabilizes formation of a mixed-valent FeII/FeIII state and enhances charge resonance stabilization of the bis-FeIV state.Combining metagenomics with metaproteomics and stable isotope probing reveals metabolic pathways used by a naturally occurring marine methylotroph.
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MauG, a diheme enzyme that catalyzes tryptophan tryptophylquinone biosynthesis by remote catalysis.
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 19 October 2013
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
MauG, a diheme enzyme that cat ...... synthesis by remote catalysis.
@en
MauG, a diheme enzyme that cat ...... synthesis by remote catalysis.
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type
label
MauG, a diheme enzyme that cat ...... synthesis by remote catalysis.
@en
MauG, a diheme enzyme that cat ...... synthesis by remote catalysis.
@nl
prefLabel
MauG, a diheme enzyme that cat ...... synthesis by remote catalysis.
@en
MauG, a diheme enzyme that cat ...... synthesis by remote catalysis.
@nl
P2860
P1476
MauG, a diheme enzyme that cat ...... synthesis by remote catalysis.
@en
P2093
Sooim Shin
P2860
P304
P356
10.1016/J.ABB.2013.10.004
P407
P577
2013-10-19T00:00:00Z