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Association of iron‐protoporphyrin‐IX (hemin) with myosins
Author(s) -
Bhoite-Solomon V.,
Kessler-Icekson G.,
Shaklai N.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)81493-8
Subject(s) - citation , protoporphyrin ix , library science , chemistry , computer science , combinatorics , mathematics , organic chemistry , photodynamic therapy
Addition of myosins isolated from guinea pig heart and rabbit skeletal muscle to hemin solutions resulted in the appearance of new absorption spectra indicating association of hemin and the myosins. Binding stoichiometry based on absorption changes was found to be two hemin sites per myosin molecule. The binding constants calculated from quenching of the intrinsic fluorescence of the myosins by hemin are Ka = 7 (+/- 2) 10(6) M-1 for skeletal muscle myosin, and Ka = 3 (+/- 1) x 10(7) M-1 for heart muscle myosin. Based on these findings, myosins are suggested as potential transporters of free hemin between cell organelles.