J.P. Hosler, S. Ferguson-Miller, M.W. Calhoun, J.W. Thomas, J. Hill, L. Lemieux, J. Ma, C. Georgiou, J. Fetter, J. Shapleigh, M.M.J. Tecklenburg, G.T. Babcock, R.B. Gennis, "Insight into the active-site structure and function of cytochrome oxidase by analysis of site-directed mutants of bacterial cytochrome aa3 and cytochrome bo," Journal of Bioenergetics and Biomembranes, 25:121-36, 1993. (Cited in 56 publications through December 1994)
Comments by Robert B. Gennis and Jonathan P. Hosler
Working with bacterial cytochrome oxidases, the authors--from three different laboratories--have made inroads into understanding the structure of the active site of an important energy-generating protein. The protein couples electron transport to proton pumping across membranes in living systems.
"This paper was the first to provide an empirically based, three-dimensional model of the portion of the enzyme where metals bind--namely its active site," says Robert Gennis, a professor of biochemistry and chemistry at the University of Illinois, Urbana-Champaign.