Circular dichroism and magnetic circular dichroism of iron-sulfur proteins. 1978

P J Stephens, and A J Thomson, and J B Dunn, and T A Keiderling, and J Rawlings, and K K Rao, and D O Hall

Circular dichroism (CD) and magnetic circular dichroism (MCD) spectra are reported for the 2-Fe ferredoxins from Pseudomonas putida and Spirulina maxima, Chromatium HIPIP, the 4-Fe ferredoxin from Bacillus stearothermophilus, and the 8-Fe ferredoxin from Clostridium pasteurianum. The spectral range spans the near-infrared, visible, and near ultraviolet. In all cases except oxidized 2-Fe ferredoxins, electronic absorption is observed continuously from less than 5000 cm-1 to above 30,000 cm-1. The CD spectra of the two 2-Fe ferredoxins are similar. In contrast, the CD of the 4-Fe and 8-Fe proteins, for a given 4-Fe cluster oxidation level, varies considerable with protein. MCD is less sensitive to protein environment than is CD. In the 2-Fe proteins, MCD at 5 T is appreciably smaller than the CD; in the 4-Fe and 8-Fe proteins, MCD and CD are comparable in magnitude. Both CD and MCD are more highly structured than the corresponding absorption spectra. The CD and MCD spectra reported provide a broader base than heretofore available for the characterization of iron-sulfur proteins containing 2-Fe and 4-Fe clusters and for the evaluation of electronic structural models for these clusters.

UI MeSH Term Description Entries
D007506 Iron-Sulfur Proteins A group of proteins possessing only the iron-sulfur complex as the prosthetic group. These proteins participate in all major pathways of electron transport: photosynthesis, respiration, hydroxylation and bacterial hydrogen and nitrogen fixation. Iron-Sulfur Protein,Iron Sulfur Proteins,Iron Sulfur Protein,Protein, Iron-Sulfur,Proteins, Iron Sulfur,Proteins, Iron-Sulfur,Sulfur Proteins, Iron
D008280 Magnetics The study of MAGNETIC PHENOMENA. Magnetic
D008667 Metalloproteins Proteins that have one or more tightly bound metal ions forming part of their structure. (Dorland, 28th ed) Metalloprotein
D009905 Optical Rotatory Dispersion The method of measuring the dispersion of an optically active molecule to determine the relative magnitude of right- or left-handed components and sometimes structural features of the molecule. Dispersion, Optical Rotatory,Rotatory Dispersion, Optical
D010084 Oxidation-Reduction A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471). Redox,Oxidation Reduction
D011487 Protein Conformation The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). Conformation, Protein,Conformations, Protein,Protein Conformations
D002942 Circular Dichroism A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed) Circular Dichroism, Vibrational,Dichroism, Circular,Vibrational Circular Dichroism
D005288 Ferredoxins Iron-containing proteins that transfer electrons, usually at a low potential, to flavoproteins; the iron is not present as in heme. (McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed) Ferredoxin,Ferredoxin I,Ferredoxin II,Ferredoxin III
D001419 Bacteria One of the three domains of life (the others being Eukarya and ARCHAEA), also called Eubacteria. They are unicellular prokaryotic microorganisms which generally possess rigid cell walls, multiply by cell division, and exhibit three principal forms: round or coccal, rodlike or bacillary, and spiral or spirochetal. Bacteria can be classified by their response to OXYGEN: aerobic, anaerobic, or facultatively anaerobic; by the mode by which they obtain their energy: chemotrophy (via chemical reaction) or PHOTOTROPHY (via light reaction); for chemotrophs by their source of chemical energy: CHEMOLITHOTROPHY (from inorganic compounds) or chemoorganotrophy (from organic compounds); and by their source for CARBON; NITROGEN; etc.; HETEROTROPHY (from organic sources) or AUTOTROPHY (from CARBON DIOXIDE). They can also be classified by whether or not they stain (based on the structure of their CELL WALLS) with CRYSTAL VIOLET dye: gram-negative or gram-positive. Eubacteria

Related Publications

P J Stephens, and A J Thomson, and J B Dunn, and T A Keiderling, and J Rawlings, and K K Rao, and D O Hall
April 1973, Biochemical and biophysical research communications,
P J Stephens, and A J Thomson, and J B Dunn, and T A Keiderling, and J Rawlings, and K K Rao, and D O Hall
January 1981, Biochemistry,
P J Stephens, and A J Thomson, and J B Dunn, and T A Keiderling, and J Rawlings, and K K Rao, and D O Hall
October 1982, Biochemical and biophysical research communications,
P J Stephens, and A J Thomson, and J B Dunn, and T A Keiderling, and J Rawlings, and K K Rao, and D O Hall
May 1981, Biochemistry,
P J Stephens, and A J Thomson, and J B Dunn, and T A Keiderling, and J Rawlings, and K K Rao, and D O Hall
July 1977, Biochimica et biophysica acta,
P J Stephens, and A J Thomson, and J B Dunn, and T A Keiderling, and J Rawlings, and K K Rao, and D O Hall
January 1976, Advances in biophysics,
P J Stephens, and A J Thomson, and J B Dunn, and T A Keiderling, and J Rawlings, and K K Rao, and D O Hall
July 1983, Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme,
P J Stephens, and A J Thomson, and J B Dunn, and T A Keiderling, and J Rawlings, and K K Rao, and D O Hall
January 1980, Nucleic acids symposium series,
P J Stephens, and A J Thomson, and J B Dunn, and T A Keiderling, and J Rawlings, and K K Rao, and D O Hall
July 1977, Biochimica et biophysica acta,
P J Stephens, and A J Thomson, and J B Dunn, and T A Keiderling, and J Rawlings, and K K Rao, and D O Hall
January 1978, Methods in enzymology,
Copied contents to your clipboard!