The menD and menE homologs code for 2-succinyl-6-hydroxyl-2,4-cyclohexadiene-1-carboxylate synthase and O-succinylbenzoic acid-CoA synthase in the phylloquinone biosynthetic pathway of Synechocystis sp. PCC 6803

T. Wade Johnson, Sushma Naithani, Charles Stewart, Boris Zybailov, A. Daniel Jones, John H. Golbeck, Parag R. Chitnis

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

The genome of the cyanobacterium Synechocystis sp. PCC 6803 contains genes identified as menD and menE, homologs of Escherichia coli genes that code for 2-succinyl-6-hydroxyl-2,4-cyclohexadiene-1-carboxylate (SHCHC) synthase and O-succinylbenzoic acid-CoA ligase in the menaquinone biosynthetic pathway. In cyanobacteria, the product of this pathway is 2-methyl-3-phytyl-1,4-naphthoquinone (phylloquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem (PS) I. The menD - and menE - strains were generated, and both were found to lack phylloquinone. Hence, no alternative pathways exist in cyanobacteria to produce O-succinylbenzoyl-CoA. Q-band EPR studies of photoaccumulated quinone anion radical and optical kinetic studies of the P700 + [F A /F B ] - backreaction indicate that in the mutant strains, plastoquinone-9 functions as the electron transfer cofactor in the A 1 site of PS I. At a light intensity of 40 μE m -2 s -1 , the menD - and menE - mutant strains grew photoautotrophically and photoheterotrophically, but with doubling times slower than the wild type. Both of which are sensitive to high light intensities. Low-temperature fluorescence studies show that in the menD - and menE - mutants, the ratio of PS I to PS II is reduced relative to the wild type. Whole-chain electron transfer rates in the menD - and menE - mutant cells are correspondingly higher on a chlorophyll basis. The slower growth rate and high-light sensitivity of the menD - and menE - mutants are therefore attributed to a lower content of PS I per cell.

Original languageEnglish (US)
Pages (from-to)67-76
Number of pages10
JournalBiochimica et Biophysica Acta - Bioenergetics
Volume1557
Issue number1-3
DOIs
StatePublished - Mar 6 2003

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Vitamin K 1
Synechocystis
Photosystem I Protein Complex
Biosynthetic Pathways
Coenzyme A
Hydroxyl Radical
Cyanobacteria
Acids
Genes
Electrons
Plastoquinone
High intensity light
Vitamin K 2
Light
Photophobia
Photosensitivity
Photosystem II Protein Complex
Chlorophyll
Ligases
Escherichia coli

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Cell Biology

Cite this

@article{67dce6b3fd484eb7ae43963c70177246,
title = "The menD and menE homologs code for 2-succinyl-6-hydroxyl-2,4-cyclohexadiene-1-carboxylate synthase and O-succinylbenzoic acid-CoA synthase in the phylloquinone biosynthetic pathway of Synechocystis sp. PCC 6803",
abstract = "The genome of the cyanobacterium Synechocystis sp. PCC 6803 contains genes identified as menD and menE, homologs of Escherichia coli genes that code for 2-succinyl-6-hydroxyl-2,4-cyclohexadiene-1-carboxylate (SHCHC) synthase and O-succinylbenzoic acid-CoA ligase in the menaquinone biosynthetic pathway. In cyanobacteria, the product of this pathway is 2-methyl-3-phytyl-1,4-naphthoquinone (phylloquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem (PS) I. The menD - and menE - strains were generated, and both were found to lack phylloquinone. Hence, no alternative pathways exist in cyanobacteria to produce O-succinylbenzoyl-CoA. Q-band EPR studies of photoaccumulated quinone anion radical and optical kinetic studies of the P700 + [F A /F B ] - backreaction indicate that in the mutant strains, plastoquinone-9 functions as the electron transfer cofactor in the A 1 site of PS I. At a light intensity of 40 μE m -2 s -1 , the menD - and menE - mutant strains grew photoautotrophically and photoheterotrophically, but with doubling times slower than the wild type. Both of which are sensitive to high light intensities. Low-temperature fluorescence studies show that in the menD - and menE - mutants, the ratio of PS I to PS II is reduced relative to the wild type. Whole-chain electron transfer rates in the menD - and menE - mutant cells are correspondingly higher on a chlorophyll basis. The slower growth rate and high-light sensitivity of the menD - and menE - mutants are therefore attributed to a lower content of PS I per cell.",
author = "Johnson, {T. Wade} and Sushma Naithani and Charles Stewart and Boris Zybailov and Jones, {A. Daniel} and Golbeck, {John H.} and Chitnis, {Parag R.}",
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The menD and menE homologs code for 2-succinyl-6-hydroxyl-2,4-cyclohexadiene-1-carboxylate synthase and O-succinylbenzoic acid-CoA synthase in the phylloquinone biosynthetic pathway of Synechocystis sp. PCC 6803. / Johnson, T. Wade; Naithani, Sushma; Stewart, Charles; Zybailov, Boris; Jones, A. Daniel; Golbeck, John H.; Chitnis, Parag R.

In: Biochimica et Biophysica Acta - Bioenergetics, Vol. 1557, No. 1-3, 06.03.2003, p. 67-76.

Research output: Contribution to journalArticle

TY - JOUR

T1 - The menD and menE homologs code for 2-succinyl-6-hydroxyl-2,4-cyclohexadiene-1-carboxylate synthase and O-succinylbenzoic acid-CoA synthase in the phylloquinone biosynthetic pathway of Synechocystis sp. PCC 6803

AU - Johnson, T. Wade

AU - Naithani, Sushma

AU - Stewart, Charles

AU - Zybailov, Boris

AU - Jones, A. Daniel

AU - Golbeck, John H.

AU - Chitnis, Parag R.

PY - 2003/3/6

Y1 - 2003/3/6

N2 - The genome of the cyanobacterium Synechocystis sp. PCC 6803 contains genes identified as menD and menE, homologs of Escherichia coli genes that code for 2-succinyl-6-hydroxyl-2,4-cyclohexadiene-1-carboxylate (SHCHC) synthase and O-succinylbenzoic acid-CoA ligase in the menaquinone biosynthetic pathway. In cyanobacteria, the product of this pathway is 2-methyl-3-phytyl-1,4-naphthoquinone (phylloquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem (PS) I. The menD - and menE - strains were generated, and both were found to lack phylloquinone. Hence, no alternative pathways exist in cyanobacteria to produce O-succinylbenzoyl-CoA. Q-band EPR studies of photoaccumulated quinone anion radical and optical kinetic studies of the P700 + [F A /F B ] - backreaction indicate that in the mutant strains, plastoquinone-9 functions as the electron transfer cofactor in the A 1 site of PS I. At a light intensity of 40 μE m -2 s -1 , the menD - and menE - mutant strains grew photoautotrophically and photoheterotrophically, but with doubling times slower than the wild type. Both of which are sensitive to high light intensities. Low-temperature fluorescence studies show that in the menD - and menE - mutants, the ratio of PS I to PS II is reduced relative to the wild type. Whole-chain electron transfer rates in the menD - and menE - mutant cells are correspondingly higher on a chlorophyll basis. The slower growth rate and high-light sensitivity of the menD - and menE - mutants are therefore attributed to a lower content of PS I per cell.

AB - The genome of the cyanobacterium Synechocystis sp. PCC 6803 contains genes identified as menD and menE, homologs of Escherichia coli genes that code for 2-succinyl-6-hydroxyl-2,4-cyclohexadiene-1-carboxylate (SHCHC) synthase and O-succinylbenzoic acid-CoA ligase in the menaquinone biosynthetic pathway. In cyanobacteria, the product of this pathway is 2-methyl-3-phytyl-1,4-naphthoquinone (phylloquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem (PS) I. The menD - and menE - strains were generated, and both were found to lack phylloquinone. Hence, no alternative pathways exist in cyanobacteria to produce O-succinylbenzoyl-CoA. Q-band EPR studies of photoaccumulated quinone anion radical and optical kinetic studies of the P700 + [F A /F B ] - backreaction indicate that in the mutant strains, plastoquinone-9 functions as the electron transfer cofactor in the A 1 site of PS I. At a light intensity of 40 μE m -2 s -1 , the menD - and menE - mutant strains grew photoautotrophically and photoheterotrophically, but with doubling times slower than the wild type. Both of which are sensitive to high light intensities. Low-temperature fluorescence studies show that in the menD - and menE - mutants, the ratio of PS I to PS II is reduced relative to the wild type. Whole-chain electron transfer rates in the menD - and menE - mutant cells are correspondingly higher on a chlorophyll basis. The slower growth rate and high-light sensitivity of the menD - and menE - mutants are therefore attributed to a lower content of PS I per cell.

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U2 - 10.1016/S0005-2728(02)00396-1

DO - 10.1016/S0005-2728(02)00396-1

M3 - Article

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AN - SCOPUS:0037422396

VL - 1557

SP - 67

EP - 76

JO - Biochimica et Biophysica Acta - Bioenergetics

JF - Biochimica et Biophysica Acta - Bioenergetics

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