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PubMed1991

Structure of the major exopolysaccharide produced by Azotobacter beijerinckii B-1615.

A. beijerinckii strain B-1615 produced two acidic exopolysaccharides in the ratio approximately 9:1. The minor polysaccharide contained mannuronic and guluronic acids in the ratio 2.3:1 and is a bacterial alginate. The major polysaccharide consisted of D-galactose, L-rhamnose, and pyruvic acid in the ratios 2:1:1 and was acetylated. On the basis of methylation analysis, and 1H- and 13C-n.m.r. spectroscopy of the polysaccharide before and after removal of the pyruvic acid residues and O-deacetylation, it was concluded that the major polysaccharide had the structure [formula; see text] with up to 1.5 OAc groups per repeating unit.

Azotobacter↗
PubMed1985

On the prosthetic group(s) of component II from nitrogenase. EPR of the Fe-protein from Azotobacter vinelandii.

The EPR spectrum of the reduced Fe-protein from nitrogenase has been reinvestigated. The dependences on temperature, microwave power, and microwave frequency all suggest that the observed signal represents a magnetically isolated [4Fe-4S]1+(2+;1+) cluster. Also, the signal can be simulated assuming a simple, g-strained S = 1/2 system. However, the integrated intensity amounts to no more than 0.2 spins per protein molecule. It is, therefore, impossible that Fe-protein preparations contain a single type of [4Fe-4S] cluster.

Azotobacter↗
PubMed1988

Time-resolved fluorescence studies on the dihydrolipoyl transacetylase (E2) component of the pyruvate dehydrogenase complex from Azotobacter vinelandii.

The dihydrolipoyl transacetylase (E2) component of A. vinelandii PDC and its lipoyl domain shows similar dynamic properties as revealed with fluorescence anisotropy decay of lipoyl-bound IAANS. The lipoyl domain (32.6 kDa), containing three almost identical subdomains shows a mode of rotation characteristic for a protein of about 30 kDa. A similar rotation is found in E2, indicating an independent rotational mobility of the whole domain in the multimeric E2 core (1.6 MDa). No independent rotation of a single lipoyl subdomain (10 kDa) is observed. The E1 component, in contrast to the E3 component, shows interaction with the lipoyl domain.

Acetyltransferases↗