Comparison with Rubredoxin

A number of techniques have contributed to the present understanding of the active site chemistry of blue copper proteins. Perhaps foremost is that involving X-ray crystallography. A wide range of physical 

The author wrishes to thank Professors E. N. Baker and G. W. Canters for information prior to publication, and Rtg, Emma, and Panos for much help and discussion. 

Results communicated at Royal Society of Chemistry (London), Annual Meeting, Belfast, April 1990 personal communication from Professor E. N. Baker. 

Reviews in Copper Proteins and Copper Enzymes (R. Lontie, ed.), Vol. 1. CRC Press, Boca Raton, Florida, 1984. 

Stigbrand, T., Biochim. Biophys. Acta 236, 246 (1971) Bergman, C., Ph.D. Thesis, Chalmers University of Technology, Gdteborg (1980). 

---

Blue copper proteins, 36 323, 377-378, see also Azurin Plastocyanin active site protonations, 36 396-398 charge, 36 398-401 classification, 36 378-379 comparison with rubredoxin, 36 404 coordinated amino acid spacing, 36 399 cucumber basic protein, 36 390 electron transfer routes, 36 403-404 electron transport, 36 378 EXAFS studies, 36 390-391 functional role, 36 382-383 occurrence, 36 379-382 properties, 36 380 pseudoazurin, 36 389-390 reduction potentials, 36 393-396 self-exchange rate constants, 36 401-403 UV-VIS spectra, 36 391-393 Blue species... 

UV-VIS Spectra Reduction Potentials Active-Site Protonations Charge on Proteins Self-Exchange Rate Constants Electron Transfer Routes Comparison with Rubredoxin Summary References... 

The unrefined structures of most proteins have been obtained by constructing physical models of perfect geometry to fit the electron density map, but this is not the case with rubredoxin. As a result, the unrefined conformation differs rather considerably from a structure with ideal geometry, more so than the conformations of other proteins described in the literature. The application of constraints on the geometric parameters should serve to make the conformation similar to that of other unrefined structures in that respect. We find that the adjustment of the unrefined structure to a reasonable model is accompanied by a decrease of the rms distance between unrefined and refined positions from 0.54 to 0.45 A (0.41 A for the main chain atoms. Those atoms for which no position is given in the unrefined structure have not been included in the comparison.)... 

Association of a rubredoxin-type center with other iron sites in proteins and structural comparisons... 

---