Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Electronic structure of the primary electron donor of Blastochloris viridis heterodimer mutants: high-field EPR study.

Biochimica et biophysica acta - 1 Sept 2010

Ponomarenko N S, Poluektov O G, Bylina E J, Norris J R

Abstract excerpt

High-field electron paramagnetic resonance (HF EPR) has been employed to investigate the primary electron donor electronic structure of Blastochloris viridis heterodimer mutant reaction centers (RCs). In these mutants the amino acid substitution His(M200)Leu or His(L173)Leu eliminates a ligand to...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Bacteriochlorophylls
Share to Electron Spin Resonance Spectroscopy
Share to Electron Transport

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Oxidation-Reduction

Share to Photosynthetic Reaction Center Complex Proteins

Share to Protein Multimerization

Source

Identifiers

PMID: 20542012
DOI: 10.1016/j.bbabio.2010.06.002

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-20542012-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Electronic structure of the primary electron donor of Blastochloris viridis heterodimer mutants: high-field EPR study.PMID 20542012Read ↗

EPR characterization of genetically modified reaction centers of Rhodobacter capsulatus.Semantic proximity Read ↗

Charge separation in Rhodobacter sphaeroides mutant reaction centers with increased midpoint potential of the primary electron donor.Semantic proximity Read ↗

Fourier transform infrared study of the primary electron donor in chromatophores of Rhodobacter sphaeroides with reaction centers genetically modified at residues M160 and L131.Semantic proximity Read ↗

Low-temperature pulsed EPR study at 34 GHz of the triplet states of the primary electron Donor P865 and the carotenoid in native and mutant bacterial reaction centers of Rhodobacter sphaeroides.Semantic proximity Read ↗

B-side charge separation in bacterial photosynthetic reaction centers: nanosecond time scale electron transfer from HB- to QB.Semantic proximity Read ↗

Conformational relaxation following reduction of the photoactive bacteriopheophytin in reaction centers from Balstochloris viridis. Influence of mutations at position M208.Semantic proximity Read ↗

Primary charge separation within P870* in wild type and heterodimer mutants in femtosecond time domain.Semantic proximity Read ↗

Comparative Study of Spectral and Functional Properties of Wild Type and Double Mutant H(L173)L/I(L177)H Reaction Centers of the Purple Bacterium Cereibacter sphaeroides.Semantic proximity Read ↗

Structural basis of the drastically increased initial electron transfer rate in the reaction center from a Rhodopseudomonas viridis mutant described at 2.00-A resolution.Semantic proximity Read ↗

Selective perturbation of the second electron transfer step in mutant bacterial reaction centers.Semantic proximity Read ↗

The electronic structure of the primary electron donor of reaction centers of purple bacteria at atomic resolution as observed by photo-CIDNP 13C NMR.Semantic proximity Read ↗

A conserved histidine-aspartate pair is required for exovinyl reduction of biliverdin by a cyanobacterial phycocyanobilin:ferredoxin oxidoreductase.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.