Life depends on transduction processes that couple cellular metabolism to e
nvironmental energy sources such as light or reduced compounds. These prima
ry energy sources must be efficiently converted into forms that can be util
ized by cells If or biosynthesis, motility, transport, regulation, and othe
r metabolic functions. In recent years, there has been an explosive increas
e in the determination of structures for proteins mediating energy transduc
tion processes. These developments provide the opportunity to evaluate the
structural basis for the efficient coupling of two energetic processes, whi
ch defines the area of structural bioenergetics. Here, we present some gene
ral features of energy transduction processes, including arguments that eff
ective coupling of two processes by a transduction protein occurs by way of
conformational States that are common to the catalysis of each process. Th
is is illustrated by examples from the nucleotide switch family of proteins
, with emphasis on the nitrogenase system where Am hydrolysis is coupled to
an: electron transfer reaction. (C) 1999 Academic Press.