Histidine ligand protonation and redox potential in the rieske dioxygenases: role of a conserved aspartate in anthranilate 1,2-dioxygenase.

Histidine ligand protonation and redox potential in the rieske dioxygenases: role of a conserved aspartate in anthranilate 1,2-dioxygenase.

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http://www.wikidata.org/entity/Q44657953
Resonance Raman studies of the (His)(Cys)3 2Fe-2S cluster of MitoNEET: comparison to the (Cys)4 mutant and implications of the effects of pH on the labile metal centerNear-IR MCD of the nonheme ferrous active site in naphthalene 1,2-dioxygenase: correlation to crystallography and structural insight into the mechanism of Rieske dioxygenases.Carnitine metabolism to trimethylamine by an unusual Rieske-type oxygenase from human microbiotaSimilar enzymes, different structures: phthalate dioxygenase is an alpha3alpha3 stacked hexamer, not an alpha3beta3 trimer like "normal" Rieske oxygenasesCharacterization of a novel Rieske-type alkane monooxygenase system in Pusillimonas sp. strain T7-7Versatility of biological non-heme Fe(II) centers in oxygen activation reactions.Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers3-Ketosteroid 9α-hydroxylase enzymes: Rieske non-heme monooxygenases essential for bacterial steroid degradation.Distal end of 105-125 loop--a putative reductase binding domain of phthalate dioxygenase.Transcriptional regulation of the ant operon, encoding two-component anthranilate 1,2-dioxygenase, on the carbazole-degradative plasmid pCAR1 of Pseudomonas resinovorans strain CA10.Rate-Determining Attack on Substrate Precedes Rieske Cluster Oxidation during Cis-Dihydroxylation by Benzoate DioxygenaseCombining steady-state and dynamic methods for determining absolute signs of hyperfine interactions: pulsed ENDOR Saturation and Recovery (PESTRE)The "bridging" aspartate 178 in phthalate dioxygenase facilitates interactions between the Rieske center and the iron(II)--mononuclear centerEngineering a three-cysteine, one-histidine ligand environment into a new hyperthermophilic archaeal Rieske-type [2Fe-2S] ferredoxin from Sulfolobus solfataricus.
P2860

Histidine ligand protonation and redox potential in the rieske dioxygenases: role of a conserved aspartate in anthranilate 1,2-dioxygenase.

Item
http://www.wikidata.org/entity/Q44657953
description
2003 nî lūn-bûn
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2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh
2003年学术文章
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@zh-hans
2003年学术文章
@zh-my
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@zh-sg
2003年學術文章
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2003年學術文章
@zh-hant
name
Histidine ligand protonation a ...... anthranilate 1,2-dioxygenase.
@en
Histidine ligand protonation a ...... anthranilate 1,2-dioxygenase.
@nl
type
label
Histidine ligand protonation a ...... anthranilate 1,2-dioxygenase.
@en
Histidine ligand protonation a ...... anthranilate 1,2-dioxygenase.
@nl
prefLabel
Histidine ligand protonation a ...... anthranilate 1,2-dioxygenase.
@en
Histidine ligand protonation a ...... anthranilate 1,2-dioxygenase.
@nl
P1433
P1476
P2093
P304
P31
P356
P407
P433
P478
P50
P577
P698
P356
P1433
P1476
Histidine ligand protonation a ...... anthranilate 1,2-dioxygenase.
@en
P2093
P304
P31
P356
P407
P433
P478
P50
P577
P698