Spectroscopic and redox properties of syml and (M)F195H: Rhodobacter capsulatus reaction center symmetry mutants which affect the initial electron donor

Jonathan W. Stocker, Aileen K W Taguchi, Heather A. Murchison, Neal W. Woodbury, Neal Woodbury

Research output: Contribution to journalArticle

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Abstract

The redox properties, absorption, electroabsorption, CD, EPR, and P+QA- recombination kinetics have been measured for the special pairs of two mutants of Rhodobacter capsulatus reaction centers involving amino acid changes in the vicinity of the special pair, P. Both mutants symmetrize amino acid residues so that portions of the M-sequence are replaced with L-sequence: syml symmetrizes all residues between M187 and M203, whereas (M)F195H is a single amino acid subset of the syml mutation. (M)-F195H introduces a His residue in a position where it is likely to form a hydrogen bond to the acetyl group of the M-side bacteriochlorophyll of P. For both mutants compared with wild-type, (i) the redox potential is at least 100 meV greater, (ii) the P+QA- recombination rate is about twice as fast at room temperature, and (iii) the large electroabsorption feature for the QY band of P is shifted relative to the absorption spectrum. The comparison of the properties observed for the syml and (M)F195H reaction center mutants and the differences between these mutants and wild-type suggest that residue M195 is an important determinant of the properties of the special pair.

Original languageEnglish (US)
Pages (from-to)10356-10362
Number of pages7
JournalBiochemistry
Volume31
Issue number42
StatePublished - 1992

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Rhodobacter capsulatus
Oxidation-Reduction
Electrons
Amino Acids
Genetic Recombination
Bacteriochlorophylls
Paramagnetic resonance
Absorption spectra
Hydrogen
Hydrogen bonds
Mutation
Kinetics
Temperature

ASJC Scopus subject areas

  • Biochemistry

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Spectroscopic and redox properties of syml and (M)F195H : Rhodobacter capsulatus reaction center symmetry mutants which affect the initial electron donor. / Stocker, Jonathan W.; Taguchi, Aileen K W; Murchison, Heather A.; Woodbury, Neal W.; Woodbury, Neal.

In: Biochemistry, Vol. 31, No. 42, 1992, p. 10356-10362.

Research output: Contribution to journalArticle

Stocker, Jonathan W. ; Taguchi, Aileen K W ; Murchison, Heather A. ; Woodbury, Neal W. ; Woodbury, Neal. / Spectroscopic and redox properties of syml and (M)F195H : Rhodobacter capsulatus reaction center symmetry mutants which affect the initial electron donor. In: Biochemistry. 1992 ; Vol. 31, No. 42. pp. 10356-10362.
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