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

Research output: Contribution to journal › Article › peer-review

87 Citations (Scopus)

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.

Original language	English
Pages (from-to)	1023-1024
Number of pages	2
Journal	Nature Structural and Molecular Biology
Volume	11
Issue number	10
DOIs	https://doi.org/10.1038/nsmb827
Publication status	Published - 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.",

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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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

N1 - M1 - Article

PY - 2004

Y1 - 2004

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.

U2 - 10.1038/nsmb827

DO - 10.1038/nsmb827

M3 - Article

SN - 1545-9993

VL - 11

SP - 1023

EP - 1024

JO - Nature Structural and Molecular Biology

JF - Nature Structural and Molecular Biology

IS - 10

ER -

Octaheme tetrathionate reductase is a respiratory enzyme with novel heme ligation

Abstract

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