Proteins, transition metal/protein

Scheme 2.19 Asymmetric reduction of alkene 46 using a hybrid transition metal/protein catalyst.

The many redox reactions that take place within a cell make use of metalloproteins with a wide range of electron transfer potentials. To name just a few of their functions, these proteins play key roles in respiration, photosynthesis, and nitrogen fixation. Some of them simply shuttle electrons to or from enzymes that require electron transfer as part of their catalytic activity. In many other cases, a complex enzyme may incorporate its own electron transfer centers. There are three general categories of transition metal redox centers cytochromes, blue copper proteins, and iron-sulfur proteins. 

Ribbon structures of two redox proteins, cytochrome c (a) and plastocyanin (b). The blowups show the active sites where transition metal atoms are located. 

The oxidation of lipids can be promoted by transition metals, such as copper or haem proteins, by a process that... 

Transition metal- or haem protein-mediated oxidative or reductive decomposition. 

The accumulation of hydroperoxides and their subsequent decomposition to alkoxyl and peroxyl radicals can accelerate the chain reaction of polyunsaturated fatty-acid p>eroxidation leading to oxidative damage to cells and membranes as well as lipoproteins. It is well-recognized that transition metals or haem proteins, through their... 

Transition metals, or haem Proteins and Ruptured Erythrocytes and Myocytes... 

Injury to cells and tissues may enhance the toxicity of the active oxygen species by releasing intracellular transition metal ions (such as iron) into the surrounding tissue from storage sites, decompartmentalized haem proteins, or metalloproteins by interaction with delocalized proteases or oxidants. Such delocalized iron and haem proteins have the capacity to decompose peroxide to peroxyl and alkoxyl radicals, exacerbating the initial lesion. 

Thus the question arises as to what forms of haem proteins and transition metals are available in vivo that are capable of mediating the formation of damaging initiating or propagating species, since the majority of the iron and haem proteins in the human body are protected in vivo from exerting pro-oxidant activities by their compart-mentalization within their functional locations in the haem and non-haem iron-containing proteins and enzymes. 

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