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Literature DB >> 5033390

Sulfheme proteins. IV. The stoichiometry of sulfur incorporation and the isolation of sulfhemin, the prosthetic group of sulfmyoglobin.

J A Berzofsky, J Peisach, B L Horecker.

Abstract

Entities: Chemical

Mesh：

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Year: 1972 PMID： 5033390

Source DB: PubMed Journal: J Biol Chem ISSN： 0021-9258 Impact factor: 5.157

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9 in total

1. NMR and EPR studies of chloroiron(III) tetraphenyl-chlorin and its complexes with imidazoles and pyridines of widely differing basicities.

Authors: Sheng Cai; Tatjana Kh Shokhireva; Dennis L Lichtenberger; F Ann Walker
Journal: Inorg Chem Date: 2006-05-01 Impact factor: 5.165

2. The Interplay between Molten Globules and Heme Disassociation Defines Human Hemoglobin Disassembly.

Authors: Premila P Samuel; Mark A White; William C Ou; David A Case; George N Phillips; John S Olson
Journal: Biophys J Date: 2020-02-04 Impact factor: 4.033

Review 3. Hydrogen sulfide and hemeproteins: knowledge and mysteries.

Authors: Ruth Pietri; Elddie Román-Morales; Juan López-Garriga
Journal: Antioxid Redox Signal Date: 2011-04-08 Impact factor: 8.401

4. Kinetic analysis of metsulphmyoglobin and metmyoglobin reduction by Fe(EDTA)2-.

Authors: A R Lim; A G Mauk
Journal: Biochem J Date: 1985-08-01 Impact factor: 3.857

5. Pro-oxidant effects of cross-linked haemoglobins explored using liposome and cytochrome c oxidase vesicle model membranes.

Authors: M S Rogers; R P Patel; B J Reeder; P Sarti; M T Wilson; A I Alayash
Journal: Biochem J Date: 1995-09-15 Impact factor: 3.857

Sulfheme proteins. IV. The stoichiometry of sulfur incorporation and the isolation of sulfhemin, the prosthetic group of sulfmyoglobin.

1. NMR and EPR studies of chloroiron(III) tetraphenyl-chlorin and its complexes with imidazoles and pyridines of widely differing basicities.

2. The Interplay between Molten Globules and Heme Disassociation Defines Human Hemoglobin Disassembly.

Review 3. Hydrogen sulfide and hemeproteins: knowledge and mysteries.

4. Kinetic analysis of metsulphmyoglobin and metmyoglobin reduction by Fe(EDTA)2-.

5. Pro-oxidant effects of cross-linked haemoglobins explored using liposome and cytochrome c oxidase vesicle model membranes.

Review 6. Chemical Biology of H₂S Signaling through Persulfidation.

Review 7. Hydrogen sulfide activation in hemeproteins: the sulfheme scenario.

8. Studies of iron(III) porphyrinates containing silanethiolate ligands.

9. Hydrosulfide (HS-) coordination in iron porphyrinates.

Sulfheme proteins. IV. The stoichiometry of sulfur incorporation and the isolation of sulfhemin, the prosthetic group of sulfmyoglobin.

1. NMR and EPR studies of chloroiron(III) tetraphenyl-chlorin and its complexes with imidazoles and pyridines of widely differing basicities.

2. The Interplay between Molten Globules and Heme Disassociation Defines Human Hemoglobin Disassembly.

Review 3. Hydrogen sulfide and hemeproteins: knowledge and mysteries.

4. Kinetic analysis of metsulphmyoglobin and metmyoglobin reduction by Fe(EDTA)2-.

5. Pro-oxidant effects of cross-linked haemoglobins explored using liposome and cytochrome c oxidase vesicle model membranes.

Review 6. Chemical Biology of H2S Signaling through Persulfidation.

Review 7. Hydrogen sulfide activation in hemeproteins: the sulfheme scenario.

8. Studies of iron(III) porphyrinates containing silanethiolate ligands.

9. Hydrosulfide (HS-) coordination in iron porphyrinates.

Review 6. Chemical Biology of H₂S Signaling through Persulfidation.