注意到 发表于 2025-3-25 06:52:57

http://reply.papertrans.cn/83/8246/824504/824504_21.png

watertight, 发表于 2025-3-25 10:22:14

http://reply.papertrans.cn/83/8246/824504/824504_22.png

MUTED 发表于 2025-3-25 13:22:39

Metalloporphyrin Films on Solid Electrodes: Reflectance Spectroscopy and AC Impedance Studies in Aqunit in heme proteins but also as potential electrocatalysts.. Metalloporphyrins have been found to be applicable in both homogeneous and heterogeneous catalysis.; and, because oxygen can be reduced directly through a 4-electron pathway on some transition metal porphyrins, catalysis in the heterogen

啪心儿跳动 发表于 2025-3-25 18:23:51

Bacterial Cytochrome P-450 Enzymes and Reactions on Immobilized Electrodes. I. Preliminary Studies,on reactions. These typical monooxygenase enzymes require the transfer of two electrons to the heme active center per molecule of substrate converted. Biochemically, electron transfer to or from the enzyme is often linked to the electron flow in the physiological cycle of a cell or microorganism thr

Gorilla 发表于 2025-3-25 20:19:17

http://reply.papertrans.cn/83/8246/824504/824504_25.png

比目鱼 发表于 2025-3-26 03:49:02

http://reply.papertrans.cn/83/8246/824504/824504_26.png

共同生活 发表于 2025-3-26 05:38:19

The Electrochemical Characterization of the Oxene Adducts of PFe(ClO4), PFeII, and PFeII(SR) [P = Termediate known as Compound I. The latter is reduced by one electron to give a red reactive intermediate, Compound II.. Both of these intermediates contain a single oxygen atom from HOOH, and Compound I is two oxidizing equivalents above the iron(III)-heme state with a magnetic moment equivalent to

CLAMP 发表于 2025-3-26 12:26:48

http://reply.papertrans.cn/83/8246/824504/824504_28.png

飞行员 发表于 2025-3-26 13:41:01

http://reply.papertrans.cn/83/8246/824504/824504_29.png

DEAWL 发表于 2025-3-26 17:03:08

http://reply.papertrans.cn/83/8246/824504/824504_30.png
页: 1 2 [3] 4 5 6 7
查看完整版本: Titlebook: Redox Chemistry and Interfacial Behavior of Biological Molecules; Glenn Dryhurst,Katsumi Niki Book 1988 Plenum Press, New York 1988 Amino