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Article

Spectroscopic and redox properties of sym1 and (M)F195H: Rhodobacter capsulatus reaction center symmetry mutants which affect the initial electron donor.

Biochemistry - 27 Oct 1992

Stocker J W, Taguchi A K, Murchison H A, Woodbury N W, Boxer S G

Abstract excerpt

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: sym1 symmetrizes all residues between M187...

Topics

Circular Dichroism
Electron Spin Resonance Spectroscopy
Electron Transport
Genes, Bacterial
Kinetics
Light-Harvesting Protein Complexes
Mutation
Oxidation-Reduction
Photosynthetic Reaction Center Complex Proteins
Plasmids

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Conformation

Rhodobacter capsulatus

Spectrophotometry

Source

Identifiers

PMID: 1329946
DOI: 10.1021/bi00157a025

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1329946-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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Spectroscopic and redox properties of sym1 and (M)F195H: Rhodobacter capsulatus reaction center symmetry mutants which affect the initial electron donor.PMID 1329946Read ↗

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