Liver microsomal cytochromes P450 (P450) are membrane-bound enzymes and play important roles in metabolisms of exogenous drugs and carcinogens as well as endogenous hormones. To understand the structure-function relationship of membrane-bound P450, we replaced amino acids of membrane-bound microsomal rat liver P450d with DNA recombinant technique by referring to the crystal structure of water-soluble bacterial P450cam and amino acid sequences of P450s. We reviewed here our recent results of how mutations influence the catalytic functions and spectral properties of P450d and discussed the active-site structure of P450d.