By John H. Golbeck
This publication summarizes the advances made within the final decade within the biophysics, biochemistry, and molecular biology of the enzyme referred to as Photosystem I, the light-induced plastocyanin: ferredoxin oxidoreductase.
This quantity is a different compilation of chapters that come with info on molecular structure, protein-pigment interactions, excitation and electron move dynamics, protein-cofactor interactions, kinetics of electron move and bioassembly of proteins and cofactors.
The quantity starts off with a sequence of historic views that supply a great history to the sector, and ends with details on modelling of light-harvesting and electron move reactions, and the evolution of the response middle. specific consciousness is paid to spectroscopy, together with the idea of the dimension and the translation of the knowledge.
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This ebook summarizes the advances made within the final decade within the biophysics, biochemistry, and molecular biology of the enzyme often called Photosystem I, the light-induced plastocyanin: ferredoxin oxidoreductase. This quantity is a different compilation of chapters that come with info on molecular structure, protein-pigment interactions, excitation and electron move dynamics, protein-cofactor interactions, kinetics of electron move and bioassembly of proteins and cofactors.
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Additional resources for Photosystem I
2. EPR spectra of the iron–sulfur centers in intact chloroplasts after reduction in the dark with hydrogen and hydrogenase in the presence of methyl viologen. The EPR spectrum was recorded at 20 K. Source: Malkin R and Bearden AJ (1971).
See Chapter 26, p. 450. Fig. 2. NMR chemical shift perturbation of Fd upon complex formation with FNR or SiR determined by measuring 2D 1 H-15 N HSQC spectra of 15 N labeled Fd. , 2001). FNR is shown in a ribbon diagram format, with its FAD prosthetic group drawn in a wire format in purple. Fd is shown in a space-filling format with its [2Fe-2S] prosthetic group shown in brown. The Fd residues that exhibit significant changes in NMR chemical shift on complex formation with FNR, all of which are located at the contact interface between the two proteins shown in green in the 3D structure of Fd.
Ferredoxins and Laccase I was introduced to iron–sulfur proteins shortly after I came to graduate school in the Department of Biochemistry at UC Berkeley in 1962. Although I had a strong interest in enzyme mechanisms, I chose to work in the laboratory of Jesse Rabinowitz, a microbial biochemist who was involved in studies of metabolic processes in the anaerobic bacteria, Clostridia. In the early 1960s, the laboratory had become involved with a new group of electron transfer proteins, the ferredoxins, which were required for a variety of biochemical reactions in Clostridia, including pyruvate oxidation and nitrogen fixation.
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