Structural and Spectroscopic Consequences of Hexacoordination of a Bacteriochlorophyll Cofactor in the Rhodobacter sphaeroides Reaction Center

D. Frolov; M. Marsh; L.I. Crouch; P.K. Fyfe; B. Robert; R. van Grondelle; A Hadfield; M.R. Jones

doi:10.1021/bi901922t

Structural and Spectroscopic Consequences of Hexacoordination of a Bacteriochlorophyll Cofactor in the Rhodobacter sphaeroides Reaction Center

D. Frolov
, M. Marsh
, L.I. Crouch
, P.K. Fyfe
, B. Robert
, R. van Grondelle
, A Hadfield
, M.R. Jones

Research output: Contribution to Journal › Article › Academic › peer-review

Abstract

The structural and functional consequences of changing the coordination state of one of the bacteriochlorophyll (BCh1) cofactors in the purple bacterial reaction center have been explored, A combination of steady state spectroscopy and X-ray crystallography was used to demonstrate that mutagenesis of residue 181 of the L-polypeptide from Phe to Arg (FL181R) causes the BCh1 at the accessory (B

Original language	English
Pages (from-to)	1882-1892
Journal	Biochemistry
Volume	49
DOIs	https://doi.org/10.1021/bi901922t
Publication status	Published - 2010

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abstract = "The structural and functional consequences of changing the coordination state of one of the bacteriochlorophyll (BCh1) cofactors in the purple bacterial reaction center have been explored, A combination of steady state spectroscopy and X-ray crystallography was used to demonstrate that mutagenesis of residue 181 of the L-polypeptide from Phe to Arg (FL181R) causes the BCh1 at the accessory (B",

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AU - Frolov, D.

AU - Marsh, M.

AU - Crouch, L.I.

AU - Fyfe, P.K.

AU - Robert, B.

AU - van Grondelle, R.

AU - Hadfield, A

AU - Jones, M.R.

PY - 2010

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AB - The structural and functional consequences of changing the coordination state of one of the bacteriochlorophyll (BCh1) cofactors in the purple bacterial reaction center have been explored, A combination of steady state spectroscopy and X-ray crystallography was used to demonstrate that mutagenesis of residue 181 of the L-polypeptide from Phe to Arg (FL181R) causes the BCh1 at the accessory (B

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JO - Biochemistry

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Structural and Spectroscopic Consequences of Hexacoordination of a Bacteriochlorophyll Cofactor in the Rhodobacter sphaeroides Reaction Center

Abstract

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