S Nagano

Preparation and reactions of myoglobin mutants bearing both proximal cysteine ligand and hydrophobic distal cavity: protein models for the active site of P-450.

K. Ishimori, Y. Watanabe, I. Morishima, 1996, Biochemistry.

Alteration of human myoglobin proximal histidine to cysteine or tyrosine by site-directed mutagenesis: characterization and their catalytic activities.

S. Adachi, K. Ishimori, Y. Watanabe, 1991, Biochemical and biophysical research communications.

X-ray crystal structure and catalytic properties of Thr252Ile mutant of cytochrome P450cam: roles of Thr252 and water in the active center.

Y Ishimura, Y Shiro, S Adachi, 2000, Journal of biochemistry.

Roles of proximal ligand in heme proteins: replacement of proximal histidine of human myoglobin with cysteine and tyrosine by site-directed mutagenesis as models for P-450, chloroperoxidase, and catalase.

T. Egawa, S. Adachi, K. Ishimori, 1993, Biochemistry.