Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 10 March 2006:
Vol. 311. no. 5766, p. 1341
DOI: 10.1126/science.311.5766.1341h
Prev | Table of Contents | Next

This Week in Science

Figure 1 In bacteria and mitochondria, a flavin cofactor within complex I of the membrane accepts reducing equivalents, converts some of the energy into a proton gradient, and passes electrons onward via a quinone carrier to other membrane-bound enzymes. Sazanov and Hinchliffe (p. 1430, published online 9 February) describe the crystal structure of the eight-subunit hydrophilic portion (the part outside the membrane) of respiratory complex I from Thermus thermophilus and describe the environments of the flavin and the nine iron-sulfur clusters that transport the electrons from the dihydronicotinamide adenine dinucleotide (NADH) binding site into the hydrophobic (proton-pumping) domain of the complex. They propose that the outermost cluster accepts the second electron from the flavin, which helps to reduce the generation of potentially deleterious reactive oxygen species.

CREDIT: SAZANOV AND HINCHLIFFE




To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)