The binding of Mn2+ and ADP to myosin

✍ Scribed by Martonosi, Anthony

• Publisher: Wiley (John Wiley & Sons)
• Year: 1975
• Tongue: English
• Weight: 427 KB
• Volume: 3
• Category: Article
• ISSN: 0091-7419
• DOI: 10.1002/jss.400030403

✦ Synopsis

Abstract

The metal ion requirement of myosin‐ADP binding was investigated by use of Mn^2+^. Mn^2+^ binds to two sets of noninteracting sites on myosin which are characterized by affinity constants of 10^6^ and 10^3^, M^−1^ at 0.016 M KCl concentration. The maximum number of sites is 2 for the high affinity and 20–25 for the low affinity set. Binding of Mn^2+^ to the high affinity sites increases the affinity of ADP binding to myosin.

F‐actin inhibits ADP binding (Kiely, B., and Martonosi, A., Biochim. Biophys. Acta 172: 158–170 [1969]), but even at F‐actin concentrations much higher than that required to saturate the actin binding sites of myosin or its proteolytic fragments, significant ADP binding remained. The actin insensitive portion of ADP binding was inhibited by 10^−4^ M inorganic pyrophosphate or ATP. The results are discussed on the basis of a model in which actin and ADP bind to myosin at distinct but interacting sites.