TY - JOUR
T1 - Proton translocation by transhydrogenase
AU - Jackson, John
PY - 2003/6/12
Y1 - 2003/6/12
N2 - Transhydrogenase, in animal mitochondria and bacteria, couples hydride transfer between NADH and NADP(+) to proton translocation across a membrane. Within the protein, the redox reaction occurs at some distance from the proton translocation pathway and coupling is achieved through conformational changes. In an 'open' conformation of transhydrogenase, in which substrate nucleotides bind and product nucleotides dissociate, the dihydronicotinamide and nicotinamide rings are held apart to block hydride transfer; in an 'occluded' conformation, they are moved into apposition to permit the redox chemistry. In the two monomers of transhydrogenase, there is a reciprocating, out-of-phase alternation of these conformations during turnover.
AB - Transhydrogenase, in animal mitochondria and bacteria, couples hydride transfer between NADH and NADP(+) to proton translocation across a membrane. Within the protein, the redox reaction occurs at some distance from the proton translocation pathway and coupling is achieved through conformational changes. In an 'open' conformation of transhydrogenase, in which substrate nucleotides bind and product nucleotides dissociate, the dihydronicotinamide and nicotinamide rings are held apart to block hydride transfer; in an 'occluded' conformation, they are moved into apposition to permit the redox chemistry. In the two monomers of transhydrogenase, there is a reciprocating, out-of-phase alternation of these conformations during turnover.
UR - http://www.scopus.com/inward/record.url?scp=0038053908&partnerID=8YFLogxK
U2 - 10.1016/S0014-5793(03)00388-0
DO - 10.1016/S0014-5793(03)00388-0
M3 - Article
C2 - 12788487
SN - 1873-3468
VL - 545
SP - 18
EP - 24
JO - FEBS Letters
JF - FEBS Letters
IS - 1
ER -