M W Makinen

Coordination environment of the active-site metal ion of liver alcohol dehydrogenase.

M. B. Yim, M. W. Makinen, M W Makinen, 1981, Proceedings of the National Academy of Sciences of the United States of America.

The second derivative electronic absorption spectrum of cytochrome c oxidase in the Soret region.

R. Copeland, M. W. Makinen, R A Copeland, 1999, Biophysical journal.

ENDOR structural characterization of a catalytically competent acylenzyme reaction intermediate of wild-type TEM-1 beta-lactamase confirms glutamate-166 as the base catalyst.

D. Mustafi, A. Sosa-Peinado, M. W. Makinen, 2001, Biochemistry.

Neutral metal-bound water is the base catalyst in liver alcohol dehydrogenase.

W. Maret, M. B. Yim, M. W. Makinen, 1983, Proceedings of the National Academy of Sciences of the United States of America.

The pH variation of steady-state kinetic parameters of site-specific Co(2+)-reconstituted liver alcohol dehydrogenase. A mechanistic probe for the assignment of metal-linked ionizations.

W. Maret, M. W. Makinen, M W Makinen, 1991, The Journal of biological chemistry.

In vivo spin-label murine pharmacodynamics using low-frequency electron paramagnetic resonance imaging.

H J Halpern, H. Halpern, Cheng Yu, 1996, Biophysical journal.

Electron microscope study of the kinetics of the fiber-to-crystal transition of sickle cell hemoglobin.

M W Makinen, S M Wilson, 1980, Proceedings of the National Academy of Sciences of the United States of America.