Oligomeric state and membrane binding behaviour of creatine kinase isoenzymes: implications for cellular function and mitochondrial structure.

The membrane binding properties of cytosolic and mitochondrial creatine kinase isoenzymes are reviewed in this article. Differences between both dimeric and octameric mitochondrial creatine kinase (Mi-CK) attached to membranes and the unbound form are elaborated with respect to possible biological function. The formation of crystalline mitochondrial inclusions under pathological conditions and its possible origin in the membrane attachment capabilities of Mi-CK are discussed.

Functional aspects of the X-ray structure of mitochondrial creatine kinase: a molecular physiology approach.

Mitochondrial creatine kinase (Mi-CK) is a central enzyme in energy metabolism of tissues with high and fluctuating energy requirements. In this review, recent progress in the functional and structural characterization of Mi-CK is summarized with special emphasis on the solved X-ray structure of chicken Mib-CK octamer (Fritz-Wolf et al., Nature 381, 341-345, 1996).

Mitochondrial creatine kinase is a prime target of peroxynitrite-induced modification and inactivation.

The reaction of peroxynitrite (PN) with sarcomeric mitochondrial creatine kinase (Mib-CK; EC 2.7.3.

Membrane-binding and lipid vesicle cross-linking kinetics of the mitochondrial creatine kinase octamer.

Mitochondrial creatine kinase (Mi-CK; EC 2.7.3.