منابع مشابه
Primary structure of alfalfa ferredoxin.
The amino acid sequences of the six peptides obtained from tryptic digests of alfalfa ferredoxin were determined by chemical and enzymic degradations. The order of tryptic peptides was established from the properties of the two segments of the succinylated protein obtained by tryptic hydrolysis at the single arginyl residue. Alfalfa ferredoxin consists of a polypeptide chain of 9’7 residues, ch...
متن کاملThe Structure of a Bacterial Ferredoxin
The structure of the bacterial ferredoxin from Peptococcus aerogenes (54 amino acids) has been determined at 2.8 A resolution. The molecule is a prolate ellipsoid with approximate dimension of 22 x 27 A. The iron and sulfur atoms are in two complexes 12 A apart with 4 iron, 4 inorganic sulfur, and 4 cysteine sulfur atoms in each. Cys 8, 11, 14, and 45 are coordinated to iron atoms in one comple...
متن کاملPrimary structure of a high potential, four-iron-sulfur ferredoxin from the photosynthetic bacterium Rhodospirillum tenue.
The amino acid sequence of a high oxidation-reduction potential iron-sulfur protein (HiPIP) isolated from the purple photosynthetic bacterium Rhodospirillum tenue has been determined. This is the smallest of the HiPIP's, containing 63 residues, with only 3 residues apparently conserved in addition to the 4 cluster-binding cysteines. A minimum of four internal genetic gaps is postulated to align...
متن کاملStructure of a 7Fe ferredoxin from Azotobacter vinelandii.
The structure of the 7Fe ferredoxin from Azotobacter vinelandii has been solved from a 3.0-A multiple isomorphous replacement map. The crystals belong to space group P43212 with a = 55.22, c = 95.20 A, and Z = 1. Heavy-atom derivatives were prepared with K2PtCl4,K2[OsO2(OH)4], and Na3RhCl6. Anomalous scattering data were collected for native (Fe) and Pt derivative crystals. The figure of merit ...
متن کاملStructure of the bacterial plant-ferredoxin receptor FusA
Iron is a limiting nutrient in bacterial infection putting it at the centre of an evolutionary arms race between host and pathogen. Gram-negative bacteria utilize TonB-dependent outer membrane receptors to obtain iron during infection. These receptors acquire iron either in concert with soluble iron-scavenging siderophores or through direct interaction and extraction from host proteins. Charact...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1969
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)91883-1