Abstract：
:The catalytic pathways of soluble methane monooxygenase (sMMO) and cytochrome P450CAM, iron-containing enzymes, are described and compared. Recent extensive density functional ab initio electronic structure calculations have revealed many similarities in a number of the key catalytic steps, as well as some important differences. A particularly interesting and significant contrast is the role played by the protein in each system. For sMMO, the protein stabilizes various species in the catalytic cycle through a series of carboxylate shifts. This process is adequately described by a relatively compact model of the active site ( approximately 100 atoms), providing a reasonable description of the energetics of hydrogen atom abstraction. For P450CAM, in contrast, the inclusion of the full protein is necessary for an accurate description of the hydrogen atom abstraction.
journal_name
Curr Opin Chem Bioljournal_title
Current opinion in chemical biologyauthors
Guallar V,Gherman BF,Lippard SJ,Friesner RAdoi
10.1016/s1367-5931(02)00310-1subject
Has Abstractpub_date
2002-04-01 00:00:00pages
236-42issue
2eissn
1367-5931issn
1879-0402pii
S1367593102003101journal_volume
6pub_type
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