Biological Inorganic Chemistry

Fe-S clusters can be found in a set of commentaries in the Journal of Biological Inorganic Chemistry 204, 210-213). 

Munoz, A., Laib, F., Petering, D.H. and Shaw, C.F. Ill (1999) Characterization of the cadmium complex of peptide 49-61 a putative nudeation center for cadmium-induced folding in rabbit liver metallothionein IIA. Journal of Biological Inorganic Chemistry, 4, 495—507. 

Perry, C.C. and Keeling-Tucker, T. (2000) Biosilicification The role of the organic matrix in structure control. Journal of Biological Inorganic Chemistry, 5, 537-550. 

Chrichton, R. R. (2007). Biological Inorganic Chemistry An Introduction. Elsevier, Amsterdam. 

Gray, H. B., Stifel, E. I., Valentine, J. S., and Bertini, I., Eds. (2006). Biological Inorganic Chemistry Structure and Reactivity. University Science Books, Sausalito, CA. 

Figure 6.5 MoFe-protein cycle for reduction and protonation of N2. (Adapted from Figure 3 of Thorneley, R. N. F. Lowe, D. J. J. Biol. Inorg. Chem., 1996, 1, 576-580. Copyright 1996, Society of Biological Inorganic Chemistry.)...

Scheme 1. Adapted with permission from Ref. (2). Copyright 2001, Society of Biological Inorganic Chemistry.

Fig. 9. Postulated oxidation state changes occurring at the Mo and Fe centers of SO during the catalytic oxidation of sulfite, and concomitant reduction of cyt c. The one-electron reduction shown with a dashed arrow connecting MoVIFem and MoVIFen can be initiated with a laser pulse, in a solution containing 5-deazariboflavin (dRF) and a sacrificial electron donor (AH2). Reprinted with permission from Ref. (20). Copyright 1999, Society of Biological Inorganic Chemistry.

For example, reviews in Topics in Biological Inorganic Chemistry, Clarke, M. J. and Sadler, P. J., Eds. Vols. 1-2 Springer-Verlag Berlin, 1999. 

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