Structural characterization and physiological function of component B from Methanosarcina thermophila

Andrew P. Clements; Robert H. White; James G. Ferry

doi:10.1007/BF00248487

Structural characterization and physiological function of component B from Methanosarcina thermophila

Andrew P. Clements, Robert H. White, James G. Ferry

Biochemistry & Molecular Biology

Research output: Contribution to journal › Article › peer-review

6 Scopus citations

Abstract

The electron donor (component B) to the methyl coenzyme M methylreductase system from Methanosarcina thermophila was isolated as the 7-methyl derivative and characterized. Gas chromatography-mass spectrometry and ¹H NMR analyses identified this derivative as 7-methylthioheptanoylthreonine phosphate (CH₃-S-HTP), indicating that the original component B had the same structure (HS-HTP) as previously determined for component B from Methanobacterium thermoautotrophicum. The heterodisulfide of HS-HTP and coenzyme M (HS-CoM, 2-mercaptoethanesulfonate) was enzymatically reduced in cell extracts using electrons supplied by either H₂ or CO, confirming that HS-HTP was a functional molecule in M. thermophila.

Original language	English (US)
Pages (from-to)	296-300
Number of pages	5
Journal	Archives of Microbiology
Volume	159
Issue number	3
DOIs	https://doi.org/10.1007/BF00248487
State	Published - Mar 1993

All Science Journal Classification (ASJC) codes

Genetics
Molecular Biology
Biochemistry
Microbiology

Access to Document

10.1007/BF00248487

Cite this

@article{8e2b289866ac4279af35125a4049ed78,

title = "Structural characterization and physiological function of component B from Methanosarcina thermophila",

abstract = "The electron donor (component B) to the methyl coenzyme M methylreductase system from Methanosarcina thermophila was isolated as the 7-methyl derivative and characterized. Gas chromatography-mass spectrometry and 1H NMR analyses identified this derivative as 7-methylthioheptanoylthreonine phosphate (CH3-S-HTP), indicating that the original component B had the same structure (HS-HTP) as previously determined for component B from Methanobacterium thermoautotrophicum. The heterodisulfide of HS-HTP and coenzyme M (HS-CoM, 2-mercaptoethanesulfonate) was enzymatically reduced in cell extracts using electrons supplied by either H2 or CO, confirming that HS-HTP was a functional molecule in M. thermophila.",

author = "Clements, {Andrew P.} and White, {Robert H.} and Ferry, {James G.}",

year = "1993",

month = mar,

doi = "10.1007/BF00248487",

language = "English (US)",

volume = "159",

pages = "296--300",

journal = "Archives of Microbiology",

issn = "0302-8933",

publisher = "Springer Science and Business Media Deutschland GmbH",

number = "3",

}

TY - JOUR

T1 - Structural characterization and physiological function of component B from Methanosarcina thermophila

AU - Clements, Andrew P.

AU - White, Robert H.

AU - Ferry, James G.

PY - 1993/3

Y1 - 1993/3

N2 - The electron donor (component B) to the methyl coenzyme M methylreductase system from Methanosarcina thermophila was isolated as the 7-methyl derivative and characterized. Gas chromatography-mass spectrometry and 1H NMR analyses identified this derivative as 7-methylthioheptanoylthreonine phosphate (CH3-S-HTP), indicating that the original component B had the same structure (HS-HTP) as previously determined for component B from Methanobacterium thermoautotrophicum. The heterodisulfide of HS-HTP and coenzyme M (HS-CoM, 2-mercaptoethanesulfonate) was enzymatically reduced in cell extracts using electrons supplied by either H2 or CO, confirming that HS-HTP was a functional molecule in M. thermophila.

AB - The electron donor (component B) to the methyl coenzyme M methylreductase system from Methanosarcina thermophila was isolated as the 7-methyl derivative and characterized. Gas chromatography-mass spectrometry and 1H NMR analyses identified this derivative as 7-methylthioheptanoylthreonine phosphate (CH3-S-HTP), indicating that the original component B had the same structure (HS-HTP) as previously determined for component B from Methanobacterium thermoautotrophicum. The heterodisulfide of HS-HTP and coenzyme M (HS-CoM, 2-mercaptoethanesulfonate) was enzymatically reduced in cell extracts using electrons supplied by either H2 or CO, confirming that HS-HTP was a functional molecule in M. thermophila.

UR - http://www.scopus.com/inward/record.url?scp=0027478841&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027478841&partnerID=8YFLogxK

U2 - 10.1007/BF00248487

DO - 10.1007/BF00248487

M3 - Article

AN - SCOPUS:0027478841

SN - 0302-8933

VL - 159

SP - 296

EP - 300

JO - Archives of Microbiology

JF - Archives of Microbiology

IS - 3

ER -

Structural characterization and physiological function of component B from Methanosarcina thermophila

Abstract

All Science Journal Classification (ASJC) codes

Access to Document

Other files and links

Fingerprint

Cite this