Abstract:
:A sequence determinant of reduction potentials is reported for bacterial [4Fe-4S]-type ferredoxins. The residue that is four residues C-terminal to the fourth ligand of either cluster is generally an alanine or a cysteine. In five experimental ferredoxin structures, the cysteine has the same structural orientation relative to the nearest cluster, which is stabilized by the SH...S bond. Although such bonds are generally considered weak, indications that Fe-S redox site sulfurs are better hydrogen-bond acceptors than most sulfurs include the numerous amide NH...S bonds noted by Adman and our quantum mechanical calculations. Furthermore, electrostatic potential calculations of 11 experimental ferredoxin structures indicate that the extra cysteine decreases the reduction potential relative to an alanine by approximately 60 mV, in agreement with experimental mutational studies. Moreover, the decrease in potential is due to a shift in the polar backbone stabilized by the SH...S bond rather than to the slightly polar cysteinyl side chain. Thus, these cysteines can "tune" the reduction potential, which could optimize electron flow in an electron transport chain. More generally, hydrogen bonds involving sulfur can be important in protein structure/function, and mutations causing polar backbone shifts can alter electrostatics and thus affect redox properties or even enzymatic activity of a protein.
journal_name
Biophys Jjournal_title
Biophysical journalauthors
Beck BW,Xie Q,Ichiye Tdoi
10.1016/s0006-3495(01)75726-8subject
Has Abstractpub_date
2001-08-01 00:00:00pages
601-13issue
2eissn
0006-3495issn
1542-0086pii
S0006-3495(01)75726-8journal_volume
81pub_type
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