Rates of electron-transfer (ET) reactions are dependent on driving force, r
eorganizational energy, distance, and the nature of the medium which the el
ectron must traverse. In kinetically complex biological systems, non-ET rea
ctions may be required to activate the system for ET and may also influence
the observed rates. Studies of ET from tryptophan tryptophylquinone to cop
per to heme in the methylamine dehydrogenase-amicyanin-cytochrome c-551i ET
complex, as well as studies of other physiologic redox protein complexes,
are used to illustrate the combination of factors which control rates of in
terprotein ET reactions.