Octaheme tetrathionate reductase is a respiratory enzyme with novel heme ligation

Christopher G Mowat; Emma Rothery; Caroline S Miles; Lisa McIver; Mary K Doherty; Katy Drewette; Paul Taylor; Malcolm D Walkinshaw; Stephen K Chapman; Graeme A Reid

doi:10.1038/nsmb827

Octaheme tetrathionate reductase is a respiratory enzyme with novel heme ligation

Christopher G Mowat
, Emma Rothery
, Caroline S Miles
, Lisa McIver
, Mary K Doherty
, Katy Drewette
, Paul Taylor
, Malcolm D Walkinshaw
, Stephen K Chapman
, Graeme A Reid

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94 引用（Scopus）

摘要

We have isolated a soluble cytochrome from Shewanella oneidensis that contains eight covalently attached heme groups and determined its crystal structure. One of these hemes exhibits novel ligation of the iron atom by the epsilon-amino group of a lysine residue, despite its attachment via a typical CXXCH motif. This heme is most likely the active site for tetrathionate reduction, a reaction catalyzed efficiently by this enzyme.

源语言	English
页（从-至）	1023-1024
页数	2
期刊	Nature Structural & Molecular Biology
卷	11
期	10
DOI	https://doi.org/10.1038/nsmb827
出版状态	Published - 10月 2004

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10.1038/nsmb827

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title = "Octaheme tetrathionate reductase is a respiratory enzyme with novel heme ligation",

abstract = "We have isolated a soluble cytochrome from Shewanella oneidensis that contains eight covalently attached heme groups and determined its crystal structure. One of these hemes exhibits novel ligation of the iron atom by the epsilon-amino group of a lysine residue, despite its attachment via a typical CXXCH motif. This heme is most likely the active site for tetrathionate reduction, a reaction catalyzed efficiently by this enzyme.",

keywords = "Binding Sites, Catalysis, Heme, Models, Molecular, Oxidoreductases, Protein Conformation, Shewanella",

author = "Mowat, \{Christopher G\} and Emma Rothery and Miles, \{Caroline S\} and Lisa McIver and Doherty, \{Mary K\} and Katy Drewette and Paul Taylor and Walkinshaw, \{Malcolm D\} and Chapman, \{Stephen K\} and Reid, \{Graeme A\}",

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doi = "10.1038/nsmb827",

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T1 - Octaheme tetrathionate reductase is a respiratory enzyme with novel heme ligation

AU - Mowat, Christopher G

AU - Rothery, Emma

AU - Miles, Caroline S

AU - McIver, Lisa

AU - Doherty, Mary K

AU - Drewette, Katy

AU - Taylor, Paul

AU - Walkinshaw, Malcolm D

AU - Chapman, Stephen K

AU - Reid, Graeme A

PY - 2004/10

Y1 - 2004/10

N2 - We have isolated a soluble cytochrome from Shewanella oneidensis that contains eight covalently attached heme groups and determined its crystal structure. One of these hemes exhibits novel ligation of the iron atom by the epsilon-amino group of a lysine residue, despite its attachment via a typical CXXCH motif. This heme is most likely the active site for tetrathionate reduction, a reaction catalyzed efficiently by this enzyme.

AB - We have isolated a soluble cytochrome from Shewanella oneidensis that contains eight covalently attached heme groups and determined its crystal structure. One of these hemes exhibits novel ligation of the iron atom by the epsilon-amino group of a lysine residue, despite its attachment via a typical CXXCH motif. This heme is most likely the active site for tetrathionate reduction, a reaction catalyzed efficiently by this enzyme.

KW - Binding Sites

KW - Catalysis

KW - Heme

KW - Models, Molecular

KW - Oxidoreductases

KW - Protein Conformation

KW - Shewanella

U2 - 10.1038/nsmb827

DO - 10.1038/nsmb827

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SN - 1545-9993

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EP - 1024

JO - Nature Structural & Molecular Biology

JF - Nature Structural & Molecular Biology

IS - 10

ER -

Octaheme tetrathionate reductase is a respiratory enzyme with novel heme ligation

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