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| SPECTROSCOPIC CHARACTERIZATION OF FE-57-RECONSTITUTED RUBRERYTHRIN, A NONHEME IRON PROTEIN WITH STRUCTURAL ANALOGIES TO RIBONUCLEOTIDE REDUCTASE |
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| Author(s): RAVI N, PRICKRIL BC, KURTZ DM, HUYNH BH |
| Source: BIOCHEMISTRY Volume: 32 Issue: 33 Pages: 8487-8491 Published: AUG 24 1993 |
| Times Cited: 26 References: 26 |
| Abstract: Rubrerythrin, a contraction of rubredoxin and hemerythrin, is the trivial name given to a non-heme iron protein isolated from Desulfovibrio vulgaris (Hildenborough). This protein, whose physiological function is unknown, was first characterized by J. LeGall et al. [(1988) Biochemistry 28, 1636] as being a homodimer of subunit M(r) = 21 900 with four Fe per homodimer distributed as two rubredoxin-type FeS4 centers and one hemerythrin-type diiron cluster. Subsequent analysis of the amino acid sequence of the rubrerythrin gene [Kurtz, D. M., Jr., & Prickril, B. C. (1991) Biochem. Biophys. Res. Commun. 181, 137] revealed an internal homology which suggested that each subunit can accommodate one diiron cluster. Here, we report a procedure for reconstitution of the as-isolated D. vulgaris rubrerythrin with Fe-57. The reconstituted protein was characterized by optical, electron paramagnetic resonance, and Mossbauer spectroscopies. The results indicate successful incorporation of Fe-57 into the two types of sites and strongly suggest that each subunit of rubrerythrin can indeed accommodate one diiron cluster as well as one rubredoxin-type center. Combined with amino acid sequence analysis, the spectroscopic characterization further suggests that the rubrerythrin subunit contains a diiron site whose structure is more closely related to that in ribonucleotide reductase than to that in hemerythrin. |
| Document Type: Article |
| Language: English |
Addresses:
1. UNIV GEORGIA, DEPT CHEM, ATHENS, GA 30602 USA
2. UNIV GEORGIA, CTR MET ENZYME STUDIES, ATHENS, GA 30602 USA
3. EMORY UNIV, DEPT PHYS, ATLANTA, GA 30322 USA |
| Publisher: AMER CHEMICAL SOC, 1155 16TH ST, NW, WASHINGTON, DC 20036 |
| Subject Category: Biochemistry & Molecular Biology |
| IDS Number: LW559 |
| ISSN: 0006-2960 |
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