Coenzyme B
Names
IUPAC name
2-[(7-mercapto-1-oxoheptyl)amino]-3-phosphonooxybutanoic acid
Identifiers
ChemSpider
UNII
InChI=1S/C11H22NO7PS/c1-8(19-20(16,17)18)10(11(14)15)12-9(13)6-4-2-3-5-7-21/h8,10,21H,2-7H2,1H3,(H,12,13)(H,14,15)(H2,16,17,18)
Y Key: JBJSVEVEEGOEBZ-UHFFFAOYSA-N
Y InChI=1/C11H22NO7PS/c1-8(19-20(16,17)18)10(11(14)15)12-9(13)6-4-2-3-5-7-21/h8,10,21H,2-7H2,1H3,(H,12,13)(H,14,15)(H2,16,17,18)/t8-,10-/m1/s1
Key: JBJSVEVEEGOEBZ-PSASIEDQBT
InChI=1/C11H22NO7PS/c1-8(19-20(16,17)18)10(11(14)15)12-9(13)6-4-2-3-5-7-21/h8,10,21H,2-7H2,1H3,(H,12,13)(H,14,15)(H2,16,17,18)
Key: JBJSVEVEEGOEBZ-UHFFFAOYAG
O=C(N[C@@H](C(=O)O)[C@H](OP(=O)(O)O)C)CCCCCCS
O=C(NC(C(=O)O)C(OP(=O)(O)O)C)CCCCCCS
Properties
C11 22 7
Molar mass
343.333641
Except where otherwise noted, data are given for materials in their
standard state (at 25 °C [77 °F], 100 kPa).
Chemical compound
Coenzyme B is a coenzyme required for redox reactions in methanogens . The full chemical name of coenzyme B is 7-mercaptoheptanoylthreoninephosphate.[ 1] thiol , which is its principal site of reaction.
Coenzyme B reacts with 2-methylthioethanesulfonate (methyl-Coenzyme M , abbreviated CH3 ), to release methane in methanogenesis :[ 2]
CH3 CH4 + CoB–S–S–CoMThis conversion is catalyzed by the enzyme methyl coenzyme M reductase , which contains cofactor F430 as the prosthetic group .
A related conversion that utilizes both HS-CoB and HS-CoM is the reduction of fumarate to succinate , catalyzed by fumarate reductase :[ 3]
HS–CoM + HS–CoB + − O2 − 2 → − O2 2 2 − 2 + CoB–S–S–CoM
Importance of coenzyme B in methanogenesis
Coenzyme B is an important component in the terminal step of methane biogenesis.[ 4] [ 5] [ 6]
References
^ Noll KM, Rinehart KL, Tanner RS, Wolfe RS (1986). "Structure of component B (7-mercaptoheptanoylthreonine phosphate) of the methylcoenzyme M methylreductase system of Methanobacterium thermoautotrophicum" . Proceedings of the National Academy of Sciences . 83 (12): 4238– 42. Bibcode :1986PNAS...83.4238N . doi :10.1073/pnas.83.12.4238 PMC 323707 PMID 3086878 . ^ Thauer RK (September 1998). "Biochemistry of methanogenesis: a tribute to Marjory Stephenson. 1998 Marjory Stephenson Prize Lecture" . Microbiology . 144 (Pt 9): 2377– 406. doi :10.1099/00221287-144-9-2377 PMID 9782487 . ^ Heim S, Künkel A, Thauer RK, Hedderich R (April 1998). "Thiol:fumarate reductase (Tfr) from Methanobacterium thermoautotrophicum—identification of the catalytic sites for fumarate reduction and thiol oxidation" . European Journal of Biochemistry . 253 (1): 292– 9. doi :10.1046/j.1432-1327.1998.2530292.x PMID 9578488 . ^ Dey, Mishtu; Li, Xianghui; Kunz, Ryan C; Ragsdale, Stephen W (2010-12-22). "Detection of Organometallic and Radical Intermediates in the Catalytic Mechanism of Methyl-Coenzyme M Reductase Using the Natural Substrate Methyl-Coenzyme M and a Coenzyme B Substrate Analogue" . Biochemistry . 49 (51): 10902– 10911. doi :10.1021/bi101562m . PMID 21090696 . [permanent dead link ] ^ Cedervall, Peder E; Dey, Mishtu; Pearson, Arwen R; Ragsdale, Stephen W; Wilmot, Carrie M (2010-07-22). "Structural Insight into Methyl-Coenzyme M Reductase Chemistry Using Coenzyme B Analogues" . Biochemistry . 49 (35): 7683– 7693. doi :10.1021/bi100458d . PMC 3098740 PMID 20707311 . ^ Horng, Yih-Chern; Becker, Donald F; Ragsdale, Stephen W (2001-10-30). "Mechanistic Studies of Methane Biogenesis by Methyl-Coenzyme M Reductase: Evidence that Coenzyme B Participates in Cleaving the C−S Bond of Methyl-Coenzyme M" . Biochemistry . 40 (43): 12875– 12885. doi :10.1021/bi011196y . PMID 11669624 . [permanent dead link ]
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