glutamic acid and bacteriopheophytin

glutamic acid has been researched along with bacteriopheophytin in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	2 (100.00)	18.2507
2000's	0 (0.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Allen, JP; Breton, J; Nabedryk, E; Williams, JC	1
Bibikova, M; Breton, J; Nabedryk, E; Oesterhelt, D	1

Other Studies

2 other study(ies) available for glutamic acid and bacteriopheophytin

Article	Year
Electrostatic influence of QA reduction on the IR vibrational mode of the 10a-ester C==O of HA demonstrated by mutations at residues Glu L104 and Trp L100 in reaction centers from Rhodobacter sphaeroides. Biochemistry, 1997, Apr-15, Volume: 36, Issue:15 Topics: Amino Acid Sequence; Electrochemistry; Esters; Glutamic Acid; Hydrogen Bonding; Mutation; Pheophytins; Photosynthetic Reaction Center Complex Proteins; Quinones; Rhodobacter sphaeroides; Spectroscopy, Fourier Transform Infrared; Tryptophan	1997
Conformational heterogeneity of the bacteriopheophytin electron acceptor HA in reaction centers from Rhodopseudomonas viridis revealed by Fourier transform infrared spectroscopy and site-directed mutagenesis. Biochemistry, 1999, Aug-31, Volume: 38, Issue:35 Topics: Amino Acid Substitution; Benzoquinones; Deuterium Oxide; Electron Transport; Glutamic Acid; Glutamine; Mutagenesis, Site-Directed; Oxidation-Reduction; Phenylalanine; Pheophytins; Photochemistry; Photosynthetic Reaction Center Complex Proteins; Protein Conformation; Protons; Rhodopseudomonas; Spectroscopy, Fourier Transform Infrared; Static Electricity; Tryptophan	1999

Article

Year

Electrostatic influence of QA reduction on the IR vibrational mode of the 10a-ester C==O of HA demonstrated by mutations at residues Glu L104 and Trp L100 in reaction centers from Rhodobacter sphaeroides.

Biochemistry, 1997, Apr-15, Volume: 36, Issue:15

Topics: Amino Acid Sequence; Electrochemistry; Esters; Glutamic Acid; Hydrogen Bonding; Mutation; Pheophytins; Photosynthetic Reaction Center Complex Proteins; Quinones; Rhodobacter sphaeroides; Spectroscopy, Fourier Transform Infrared; Tryptophan

1997

Conformational heterogeneity of the bacteriopheophytin electron acceptor HA in reaction centers from Rhodopseudomonas viridis revealed by Fourier transform infrared spectroscopy and site-directed mutagenesis.

Biochemistry, 1999, Aug-31, Volume: 38, Issue:35

Topics: Amino Acid Substitution; Benzoquinones; Deuterium Oxide; Electron Transport; Glutamic Acid; Glutamine; Mutagenesis, Site-Directed; Oxidation-Reduction; Phenylalanine; Pheophytins; Photochemistry; Photosynthetic Reaction Center Complex Proteins; Protein Conformation; Protons; Rhodopseudomonas; Spectroscopy, Fourier Transform Infrared; Static Electricity; Tryptophan

1999