Alkane-Oxidizing Enzyme AlkB
Rachel N Austin
Department of Chemistry, Barnard College, Columbia University, New York, NY, 10027 USA
Search for more papers by this authorClorice R Reinhardt
Department of Chemical Engineering, Massachusetts Institute of Technology, Cambridge, MA, 02139 USA
Search for more papers by this authorLiang Feng
Department of Molecular and Cellular Physiology, Stanford University, Stanford, CA, 94305 USA
Search for more papers by this authorRachel N Austin
Department of Chemistry, Barnard College, Columbia University, New York, NY, 10027 USA
Search for more papers by this authorClorice R Reinhardt
Department of Chemical Engineering, Massachusetts Institute of Technology, Cambridge, MA, 02139 USA
Search for more papers by this authorLiang Feng
Department of Molecular and Cellular Physiology, Stanford University, Stanford, CA, 94305 USA
Search for more papers by this authorAbstract
Alkanotrophs are microorganisms capable of utilizing alkanes as their sole source of carbon and energy. Alkane monooxygenase (AlkB) is a membrane-spanning diiron monooxygenase used by many alkanotrophs, in a variety of environments, to catalyze the conversion of straight-chain alkanes from C5 to C32 to the corresponding terminal alcohol. AlkB has a narrow substrate channel, capable of accommodating linear alkanes. Multiple lines of evidence support the assertion that subtle changes in the structure of the substrate channel shift the range of alkyl chain lengths favored by a particular AlkB isoform. The active site of AlkB contains two iron ions coordinated by nine histidines. No covalent bridge connects the two iron ions. The active site is similar to that of other class-III diiron enzymes including fatty acid desaturases and fatty acid hydroxylases, but different from that of other nonheme diiron enzymes, and raises questions about the mechanisms used to activate O2 and inert CH bonds.
3D Structure
References
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