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Literature DB >> 5240016

Mössbauer studies on putidaredoxin.

R Cooke, J C Tsibris, P G Debrunner, R Tsai, I C Gunsalus, H Frauenfelder.

Abstract

Mesh：

Substances：
Sulfides
Iron
Oxygenases

Year: 1968 PMID： 5240016 PMCID： PMC224828 DOI： 10.1073/pnas.59.4.1045

Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205

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6 in total

1. THE NATURE OF IRON IN FERREDOXIN.

Authors: D C BLOMSTROM; E KNIGHT; W D PHILLIPS; J F WEIHER
Journal: Proc Natl Acad Sci U S A Date: 1964-06 Impact factor: 11.205

2. The ferroprotein component of a methylene hydroxylase.

Authors: D W Cushman; R L Tsai; I C Gunsalus
Journal: Biochem Biophys Res Commun Date: 1967-03-09 Impact factor: 3.575

3. The iron complex in spinach ferredoxin.

Authors: J F Gibson; D O Hall; J H Thornley; F R Whatley
Journal: Proc Natl Acad Sci U S A Date: 1966-09 Impact factor: 11.205

4. Identification of sulfur as component of the EPR signal at g equals 1.94 by isotopic substitution.

Authors: D V DerVartanian; W H Orme-Johnson; R E Hansen; H Beinert
Journal: Biochem Biophys Res Commun Date: 1967-03-09 Impact factor: 3.575

5. On the ligand field of iron in ferredoxin from spinach chloroplasts and related nonheme iron enzymes.

Authors: H Brintzinger; G Palmer; R H Sands
Journal: Proc Natl Acad Sci U S A Date: 1966-02 Impact factor: 11.205

6. The number of iron atoms in the paramagnetic center (G =1.94) of reduced putidaredoxin, a nonheme iron protein.

Authors: J C Tsibris; R L Tsai; I C Gunsalus; W H Orme-Johnson; R E Hansen; H Beinert
Journal: Proc Natl Acad Sci U S A Date: 1968-03 Impact factor: 11.205

6 in total

5 in total

Mössbauer studies on putidaredoxin.

1. THE NATURE OF IRON IN FERREDOXIN.

2. The ferroprotein component of a methylene hydroxylase.

3. The iron complex in spinach ferredoxin.

4. Identification of sulfur as component of the EPR signal at g equals 1.94 by isotopic substitution.

5. On the ligand field of iron in ferredoxin from spinach chloroplasts and related nonheme iron enzymes.

6. The number of iron atoms in the paramagnetic center (G =1.94) of reduced putidaredoxin, a nonheme iron protein.

1. [Ferredoxin from Bumilleriopsis filiformis Vischer].

2. Structure and reactions of oxygenase active centres: cytochrome P-450 and iron-sulphur proteins.

3. Biological electron transport systems.

4. Mossbauer spectroscopy of the iron-sulfur proteins.

5. Mössbauer studies of adrenodoxin. The mechanism of electron transfer in a hydroxylase iron-sulphur protein.