The manganese stabilising protein (MSP) of Prochlorothrix hollandica is a hydrophobic membrane-bound protein

Tsafrir S. Mor; Anton F. Post; Itzhak Ohad

doi:10.1016/0005-2728(93)90044-G

The manganese stabilising protein (MSP) of Prochlorothrix hollandica is a hydrophobic membrane-bound protein

Tsafrir S. Mor, Anton F. Post, Itzhak Ohad

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

12 Scopus citations

Abstract

The oxygen-evolving Photosystem II complex of the chlorophyll-a b-containing prokaryote Prochlorothrix hollandica is similar to that of cyanobacteria in terms of the absence of the 23 kDa extrinsic polypeptide. In contrast to cyanobacteria and green chloroplasts, the manganese stabilizing protein (MSP) of Prochlorothrix is a hydrophobic protein as detected by Triton X-114 phase partitioning and has an apparent molecular mass of 37 kDa. The catalytic site of water oxidation in Prochlorothrix thylakoids is significantly more resistant to inhibition by hydroxylamine as compared with thylakoids of Chlamydomonas or Synechocystis 6803. These results indicate that the properties of the donor side of Photosystem II complex of Prochlorothrix differ from that of the related cyanobacteria.

Original language	English (US)
Pages (from-to)	206-212
Number of pages	7
Journal	BBA - Bioenergetics
Volume	1141
Issue number	2-3
DOIs	https://doi.org/10.1016/0005-2728(93)90044-G
State	Published - Mar 1 1993
Externally published	Yes

Keywords

(Prochlorothrix)
Manganese stabilizing protein
Oxygen evolving complex
Photosystem II

ASJC Scopus subject areas

Biophysics
Biochemistry
Cell Biology

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10.1016/0005-2728(93)90044-G

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title = "The manganese stabilising protein (MSP) of Prochlorothrix hollandica is a hydrophobic membrane-bound protein",

abstract = "The oxygen-evolving Photosystem II complex of the chlorophyll-a b-containing prokaryote Prochlorothrix hollandica is similar to that of cyanobacteria in terms of the absence of the 23 kDa extrinsic polypeptide. In contrast to cyanobacteria and green chloroplasts, the manganese stabilizing protein (MSP) of Prochlorothrix is a hydrophobic protein as detected by Triton X-114 phase partitioning and has an apparent molecular mass of 37 kDa. The catalytic site of water oxidation in Prochlorothrix thylakoids is significantly more resistant to inhibition by hydroxylamine as compared with thylakoids of Chlamydomonas or Synechocystis 6803. These results indicate that the properties of the donor side of Photosystem II complex of Prochlorothrix differ from that of the related cyanobacteria.",

keywords = "(Prochlorothrix), Manganese stabilizing protein, Oxygen evolving complex, Photosystem II",

author = "Mor, {Tsafrir S.} and Post, {Anton F.} and Itzhak Ohad",

note = "Funding Information: This work was supported by a grant awarded by the Israel-American Binational Science Foundation, No. 88-00341. The authors wish to thank Dr. A. Gal and Dr. I. Adan~ska for their practical advice and critical reading of the manuscript.",

year = "1993",

month = mar,

day = "1",

doi = "10.1016/0005-2728(93)90044-G",

language = "English (US)",

volume = "1141",

pages = "206--212",

journal = "Biochimica et Biophysica Acta - Bioenergetics",

issn = "0005-2728",

publisher = "Elsevier",

number = "2-3",

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TY - JOUR

T1 - The manganese stabilising protein (MSP) of Prochlorothrix hollandica is a hydrophobic membrane-bound protein

AU - Mor, Tsafrir S.

AU - Post, Anton F.

AU - Ohad, Itzhak

N1 - Funding Information: This work was supported by a grant awarded by the Israel-American Binational Science Foundation, No. 88-00341. The authors wish to thank Dr. A. Gal and Dr. I. Adan~ska for their practical advice and critical reading of the manuscript.

PY - 1993/3/1

Y1 - 1993/3/1

N2 - The oxygen-evolving Photosystem II complex of the chlorophyll-a b-containing prokaryote Prochlorothrix hollandica is similar to that of cyanobacteria in terms of the absence of the 23 kDa extrinsic polypeptide. In contrast to cyanobacteria and green chloroplasts, the manganese stabilizing protein (MSP) of Prochlorothrix is a hydrophobic protein as detected by Triton X-114 phase partitioning and has an apparent molecular mass of 37 kDa. The catalytic site of water oxidation in Prochlorothrix thylakoids is significantly more resistant to inhibition by hydroxylamine as compared with thylakoids of Chlamydomonas or Synechocystis 6803. These results indicate that the properties of the donor side of Photosystem II complex of Prochlorothrix differ from that of the related cyanobacteria.

AB - The oxygen-evolving Photosystem II complex of the chlorophyll-a b-containing prokaryote Prochlorothrix hollandica is similar to that of cyanobacteria in terms of the absence of the 23 kDa extrinsic polypeptide. In contrast to cyanobacteria and green chloroplasts, the manganese stabilizing protein (MSP) of Prochlorothrix is a hydrophobic protein as detected by Triton X-114 phase partitioning and has an apparent molecular mass of 37 kDa. The catalytic site of water oxidation in Prochlorothrix thylakoids is significantly more resistant to inhibition by hydroxylamine as compared with thylakoids of Chlamydomonas or Synechocystis 6803. These results indicate that the properties of the donor side of Photosystem II complex of Prochlorothrix differ from that of the related cyanobacteria.

KW - (Prochlorothrix)

KW - Manganese stabilizing protein

KW - Oxygen evolving complex

KW - Photosystem II

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U2 - 10.1016/0005-2728(93)90044-G

DO - 10.1016/0005-2728(93)90044-G

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AN - SCOPUS:0027512601

VL - 1141

SP - 206

EP - 212

JO - Biochimica et Biophysica Acta - Bioenergetics

JF - Biochimica et Biophysica Acta - Bioenergetics

SN - 0005-2728

IS - 2-3

ER -

The manganese stabilising protein (MSP) of Prochlorothrix hollandica is a hydrophobic membrane-bound protein

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

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