Structure and mechanism in the bacterial dihaem cytochrome c peroxidases.
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Crystal Structure and Biophysical Properties of Bacillus subtilis BdbD: AN OXIDIZING THIOL:DISULFIDE OXIDOREDUCTASE CONTAINING A NOVEL METAL SITEIn Crystallo Posttranslational Modification Within a MauG/Pre-Methylamine Dehydrogenase ComplexCrystal Structures of CO and NO Adducts of MauG in Complex with Pre-Methylamine Dehydrogenase: Implications for the Mechanism of Dioxygen ActivationInvestigation of the Electron Transport Chain to and the Catalytic Activity of the Diheme Cytochrome c Peroxidase CcpA of Shewanella oneidensisMacA is a Second Cytochrome c Peroxidase of Geobacter sulfurreducensStructure of the processive rubber oxygenase RoxA from Xanthomonas spCarboxyl Group of Glu113 Is Required for Stabilization of the Diferrous and Bis-Fe IV States of MauGMauG: a di-heme enzyme required for methylamine dehydrogenase maturation.A catalytic di-heme bis-Fe(IV) intermediate, alternative to an Fe(IV)=O porphyrin radical.The diheme cytochrome c peroxidase from Shewanella oneidensis requires reductive activationUncovering novel biochemistry in the mechanism of tryptophan tryptophylquinone cofactor biosynthesis.Multi-heme proteins: nature's electronic multi-purpose toolImpact of quaternary structure upon bacterial cytochrome c peroxidases: does homodimerization matter?Prostaglandin H synthase: resolved and unresolved mechanistic issues.MauG, a diheme enzyme that catalyzes tryptophan tryptophylquinone biosynthesis by remote catalysis.Actinobacterial peroxidases: an unexplored resource for biocatalysis.Bis-Fe(IV): nature's sniper for long-range oxidation.Iron management and production of electricity by microorganisms.Predicting Protein-Protein Interactions Using BiGGER: Case Studies.Kinetic mechanism for the initial steps in MauG-dependent tryptophan tryptophylquinone biosynthesisSuicide inactivation of MauG during reaction with O(2) or H(2)O(2) in the absence of its natural protein substrate.The tightly bound calcium of MauG is required for tryptophan tryptophylquinone cofactor biosynthesis.Long-range electron transfer reactions between hemes of MauG and different forms of tryptophan tryptophylquinone of methylamine dehydrogenase.Biochemistry. Remote enzyme microsurgery.Oxidation triggers extensive conjugation and unusual stabilization of two di-heme dication diradical intermediates: role of bridging group for electronic communication.
P2860
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P2860
Structure and mechanism in the bacterial dihaem cytochrome c peroxidases.
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2006 nî lūn-bûn
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name
Structure and mechanism in the bacterial dihaem cytochrome c peroxidases.
@ast
Structure and mechanism in the bacterial dihaem cytochrome c peroxidases.
@en
type
label
Structure and mechanism in the bacterial dihaem cytochrome c peroxidases.
@ast
Structure and mechanism in the bacterial dihaem cytochrome c peroxidases.
@en
prefLabel
Structure and mechanism in the bacterial dihaem cytochrome c peroxidases.
@ast
Structure and mechanism in the bacterial dihaem cytochrome c peroxidases.
@en
P1476
Structure and mechanism in the bacterial dihaem cytochrome c peroxidases
@en
P2093
Graham W Pettigrew
P304
P356
10.1016/J.JINORGBIO.2005.12.008
P577
2006-01-24T00:00:00Z