Purification and characterization of methyl chloride transferase: A novel halogenating enzyme

Methyl Chloride is biologically produced at an annual global emission rate of $5\times10\sp6$ tons. Production of this molecule is thought to be mostly biological in nature. The established route for production of halometabolites is the hydrogen peroxide-dependent halogenation mechanism common to haloperoxidase enzymes such as chloroperoxidase. No production of monohalomethanes can be detected by the haloperoxidase mechanism. The white rot fungus, Phellinus pomaceus has been known to produce methyl chloride in vivo. After determining appropriate growth conditions for optimal methyl chloride production, we have partially purified an enzyme from this fungus which produces methyl chloride. This enzyme utilizes S-adenosyl methionine (SAM) as a methyl donor in a methyl transferase reaction in which chloride, bromide and iodide are all methyl acceptors.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Biochemistry

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2011

Author dc:creator

• Wuosmaa, Annemarie

Contributors dc:contributor

• Hager, Lowell P.

• Chemistry, Biochemistry

Statement dc:rights

• Copyright 1994 Wuosmaa, Annemarie

Language dc:language

eng

Identifier

AAI9512602
(UMI)AAI9512602

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/19956