Hasegawa T, Sadano H, Omura T
J Biochem. 1984 Jul;96(1):265-8. doi: 10.1093/oxfordjournals.jbchem.a134822.
The absorption spectrum of reduced H-450 was reversibly affected by a pH change; the Soret peak of the alkaline form was at 448 nm, and that of the acidic form (H-420) at 425 nm. The same spectral change of conversion of reduced H-450 to H-420 was also produced by the action of n-butanol, urea and p-chloromercuribenzoate. These spectral properties of H-450 were similar to those of the conversion of cytochrome P-450 to cytochrome P-420, suggesting the similar heme environments of these two hemoproteins. Reduced H-450 bound carbon monoxide to be transformed into a new spectral species having a Soret peak at 420 nm.
还原型H - 450的吸收光谱会受到pH变化的可逆影响;碱性形式的Soret峰在448nm处,酸性形式(H - 420)的Soret峰在425nm处。正丁醇、尿素和对氯汞苯甲酸的作用也会使还原型H - 450转化为H - 420产生相同的光谱变化。H - 450的这些光谱特性与细胞色素P - 450转化为细胞色素P - 420的光谱特性相似,表明这两种血红素蛋白具有相似的血红素环境。还原型H - 450与一氧化碳结合后会转化为一种新的光谱物种,其Soret峰在420nm处。