Research ExplorerPublicationsAerobic synthesis of vitamin B12

Aerobic synthesis of vitamin B12

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Aerobic synthesis of vitamin B12 : ring contraction and cobalt chelation. / Heldt, D; Lawrence, A D; Lindenmeyer, M; Deery, E; Heathcote, P; Rigby, S E; Warren, M J.

In: BIOCHEM SOC T, Vol. 33, No. Pt 4, 08.2005, p. 815-9.

Research output: SCORING: Contribution to journal › SCORING: Review article › Research

Harvard

Heldt, D, Lawrence, AD, Lindenmeyer, M, Deery, E, Heathcote, P, Rigby, SE & Warren, MJ 2005, 'Aerobic synthesis of vitamin B12: ring contraction and cobalt chelation', BIOCHEM SOC T, vol. 33, no. Pt 4, pp. 815-9. https://doi.org/10.1042/BST0330815

APA

Heldt, D., Lawrence, A. D., Lindenmeyer, M., Deery, E., Heathcote, P., Rigby, S. E., & Warren, M. J. (2005). Aerobic synthesis of vitamin B12: ring contraction and cobalt chelation. BIOCHEM SOC T, 33(Pt 4), 815-9. https://doi.org/10.1042/BST0330815

Vancouver

Heldt D, Lawrence AD, Lindenmeyer M, Deery E, Heathcote P, Rigby SE et al. Aerobic synthesis of vitamin B12: ring contraction and cobalt chelation. BIOCHEM SOC T. 2005 Aug;33(Pt 4):815-9. https://doi.org/10.1042/BST0330815

Bibtex

@article{247dfa82eccf4a58809fdb99d61affb5,
title = "Aerobic synthesis of vitamin B12: ring contraction and cobalt chelation",
abstract = "The aerobic biosynthetic pathway for vitamin B12 (cobalamin) biosynthesis is reviewed. Particular attention is focused on the ring contraction process, whereby an integral carbon atom of the tetrapyrrole-derived macrocycle is removed. Previous work had established that this chemically demanding step is facilitated by the action of a mono-oxygenase called CobG, which generates a hydroxy lactone intermediate. This mono-oxygenase contains both a non-haem iron and an Fe-S centre, but little information is known about its mechanism. Recent work has established that in bacteria such as Rhodobacter capsulatus, CobG is substituted by an isofunctional protein called CobZ. This protein has been shown to contain flavin, haem and Fe-S centres. A mechanism is proposed to explain the function of CobZ. Another interesting aspect of the aerobic cobalamin biosynthetic pathway is cobalt insertion, which displays some similarity to the process of magnesium chelation in chlorophyll synthesis. The genetic requirements of cobalt chelation and the subsequent reduction of the metal ion are discussed.",
keywords = "Aerobiosis, Bacterial Proteins, Chelating Agents, Cobalt, Models, Molecular, Oxygenases, Uroporphyrinogens, Vitamin B 12, Journal Article, Review",
author = "D Heldt and Lawrence, {A D} and M Lindenmeyer and E Deery and P Heathcote and Rigby, {S E} and Warren, {M J}",
year = "2005",
month = aug,
doi = "10.1042/BST0330815",
language = "English",
volume = "33",
pages = "815--9",
journal = "BIOCHEM SOC T",
issn = "0300-5127",
publisher = "PORTLAND PRESS LTD",
number = "Pt 4",

}

RIS

TY - JOUR

T1 - Aerobic synthesis of vitamin B12

T2 - ring contraction and cobalt chelation

AU - Heldt, D

AU - Lawrence, A D

AU - Lindenmeyer, M

AU - Deery, E

AU - Heathcote, P

AU - Rigby, S E

AU - Warren, M J

PY - 2005/8

Y1 - 2005/8

N2 - The aerobic biosynthetic pathway for vitamin B12 (cobalamin) biosynthesis is reviewed. Particular attention is focused on the ring contraction process, whereby an integral carbon atom of the tetrapyrrole-derived macrocycle is removed. Previous work had established that this chemically demanding step is facilitated by the action of a mono-oxygenase called CobG, which generates a hydroxy lactone intermediate. This mono-oxygenase contains both a non-haem iron and an Fe-S centre, but little information is known about its mechanism. Recent work has established that in bacteria such as Rhodobacter capsulatus, CobG is substituted by an isofunctional protein called CobZ. This protein has been shown to contain flavin, haem and Fe-S centres. A mechanism is proposed to explain the function of CobZ. Another interesting aspect of the aerobic cobalamin biosynthetic pathway is cobalt insertion, which displays some similarity to the process of magnesium chelation in chlorophyll synthesis. The genetic requirements of cobalt chelation and the subsequent reduction of the metal ion are discussed.

AB - The aerobic biosynthetic pathway for vitamin B12 (cobalamin) biosynthesis is reviewed. Particular attention is focused on the ring contraction process, whereby an integral carbon atom of the tetrapyrrole-derived macrocycle is removed. Previous work had established that this chemically demanding step is facilitated by the action of a mono-oxygenase called CobG, which generates a hydroxy lactone intermediate. This mono-oxygenase contains both a non-haem iron and an Fe-S centre, but little information is known about its mechanism. Recent work has established that in bacteria such as Rhodobacter capsulatus, CobG is substituted by an isofunctional protein called CobZ. This protein has been shown to contain flavin, haem and Fe-S centres. A mechanism is proposed to explain the function of CobZ. Another interesting aspect of the aerobic cobalamin biosynthetic pathway is cobalt insertion, which displays some similarity to the process of magnesium chelation in chlorophyll synthesis. The genetic requirements of cobalt chelation and the subsequent reduction of the metal ion are discussed.

KW - Aerobiosis

KW - Bacterial Proteins

KW - Chelating Agents

KW - Cobalt

KW - Models, Molecular

KW - Oxygenases

KW - Uroporphyrinogens

KW - Vitamin B 12

KW - Journal Article

KW - Review

U2 - 10.1042/BST0330815

DO - 10.1042/BST0330815

M3 - SCORING: Review article

C2 - 16042605

VL - 33

SP - 815

EP - 819

JO - BIOCHEM SOC T

JF - BIOCHEM SOC T

SN - 0300-5127

IS - Pt 4

ER -