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3 results on '"Wu, Shu-Pao"'

1. Iron-sulfur cluster biosynthesis. Kinetic analysis of [2Fe-2S] cluster transfer from holo ISU to apo Fd: role of redox chemistry and a conserved aspartate

Author

Wu, Shu-pao, Wu, Gong, Surerus, Kristene K., and Cowan, J. A.

Subjects
Biochemistry -- Research, Iron -- Physiological aspects, Sulfur -- Physiological aspects, Oxidation-reduction reaction -- Analysis, Aspartate -- Physiological aspects, Bacterial proteins -- Genetic aspects, Messenger RNA -- Genetic aspects, Genetic transcription -- Physiological aspects, Biological sciences, Chemistry
Abstract

Research has been conducted on the 2Fe and 4Fe iron (super)- cluster centers in eukaryotic organisms. The biosynthetic apparatus for these cluster center assembly has been investigated and the results indicate that the assembly of the clusters can occur only in the mitochondrion with the proteins imported from the nuclear transcribed mRNA.

Published
2002

2. Characterization of an iron-sulfur cluster assembly protein (ISU1) from Schizosaccharomyces pombe

Author

Wu, Gong, Mansy, Sheref S., Wu, Shu-pao, Surerus, Kristene K., Foster, Matthew W., and Cowan, J.A.

Subjects
Proteins -- Structure, Structure-activity relationships (Biochemistry) -- Analysis, Yeast -- Research, Metalloproteins -- Analysis, Biological sciences, Chemistry
Abstract

A working model for iron-sulfur cluster assembly protein is presented using the recombinat purified yeast protein. Data suggest that yeast protein is sparingly soluble at ambient temperatures, is sensitive to proton-mediated degradation, and forms a complex with the electron transport protein ferredoxin in both apo and holo states.

Published
2002

3. Iron-sulfur cluster biosynthesis. A comparative kinetic analysis of native and Cys-substituted ISA-mediated [2Fe-2S](sup)2+ cluster transfer to an apoferredoxin target

Author

Wu, Shu-pao and Cowan, J.A.

Subjects
Binding sites (Biochemistry) -- Analysis, Protein binding -- Analysis, Proteins -- Physiological aspects, Proteins -- Analysis, Chemical reaction, Rate of -- Analysis, Protein biosynthesis -- Research, Biological sciences, Chemistry
Abstract

Results discuss the kinetics of cluster transfer from ISA type proteins to a ferredoxin target. Data show that the rate of cluster transfer from ISA and ISU to apo-ferredoxin in the same source species are similar at physiological temperatures. However, there is a major difference in this transfer, which is the binding recognition site on the target ferredoxin.

Published
2003

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