SYNTHESIS AND PROPERTIES OF METAL-SUBSTITUTED MYOGLOBINS
SYNTHESIS AND PROPERTIES OF METAL-SUBSTITUTED MYOGLOBINS
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DOI：
10.1021/ic00310a013
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发表时间：
1989-05-31
影响因子：
4.6
通讯作者：
GRAY, HB
中科院分区：
文献类型：
--
作者：
COWAN, JA;GRAY, HB
合成了含有多种金属卟啉（MgP、CdP、SnP、PtP、PdP、H2P）的肌红蛋白，并对其进行了表征。镉被发现是一种方便的金属离子，可以直接插入或从蛋白质结合的卟啉中去除。SnMb的光化学不稳定性可能与Sn配位环境中近端组氨酸和远端组氨酸的存在有关。ZnMb（-0.80）、MgMb（-0.79）、CdMb（-0.77）、PtMb（-0.65）、PdMb（-0.62）和H？Mb （-0.45 V vs NHE）。在MgMb中观察到的延迟荧光很可能是由于卟啉所在的蛋白质袋的刚性导致了非辐射衰减率的降低。
Myoglobins containing a variety of metallomesoporphyrins (MgP, CdP, SnP, PtP, PdP, H2P) have been synthesized and char-acterized. Cadmium was found to be a convenient metal ion for direct insertion or removal from a protein-bound porphyrin. The photochemical instability of SnMb is likely relatedto the presence of both the proximal and distal histidines in the coordination environment of the Sn. Radical-cation (MP+)/excited-state (1 23MP*) reduction potentials [£(MP+/3 5MP*)] have been estimated for ZnMb (-0.80), MgMb (-0.79), CdMb (-0.77), PtMb (-0.65), PdMb (-0.62), and H? Mb (-0.45 V vs NHE). The observation of delayed fluorescence in MgMb most likely results from a reduction in the nonradiative decayrate attributable to the rigidity of the protein pocket in which the porphyrin is held.