How Do Electrostatic Perturbations of the Protein Affect the Bifurcation Pathways of Substrate Hydroxylation versus Desaturation in the Nonheme Iron-Dependent Viomycin Biosynthesis Enzyme?

2021 ◽  
Vol 125 (8) ◽  
pp. 1720-1737
Author(s):  
Hafiz Saqib Ali ◽  
Richard H. Henchman ◽  
Jim Warwicker ◽  
Sam P. de Visser
Keyword(s):  
Nonheme Iron ◽  
Substrate Hydroxylation

pH Changes That Induce an Axial Ligand Effect on Nonheme Iron(IV) Oxo Complexes with an Appended Aminopropyl Functionality

2021 ◽  
Author(s):  
Reza Latifi ◽  
Taryn D. Palluccio ◽  
Wanhua Ye ◽  
Jennifer L. Minnick ◽  
Kwame S. Glinton ◽  
...  
Keyword(s):  
Axial Ligand ◽  
Nonheme Iron ◽  
Ligand Effect ◽  
Ph Changes ◽  
Oxo Complexes

scholarly journals Obesity-Related Hypoferremia Is Not Explained by Differences in Reported Intake of Heme and Nonheme Iron or Intake of Dietary Factors that Can Affect Iron Absorption

2008 ◽  
Vol 108 (1) ◽  
pp. 145-148 ◽  
Author(s):  
Carolyn M. Menzie ◽  
Lisa B. Yanoff ◽  
Blakeley I. Denkinger ◽  
Teresa McHugh ◽  
Nancy G. Sebring ◽  
...  
Keyword(s):  
Iron Absorption ◽  
Nonheme Iron ◽  
Dietary Factors

Reaction Mechanism of a Nonheme Iron Enzyme Catalyzed Oxidative Cyclization via C–C Bond Formation

2018 ◽  
Vol 21 (1) ◽  
pp. 228-232 ◽  
Author(s):  
Wei-chen Chang ◽  
Zhi-Jie Yang ◽  
Yueh-Hua Tu ◽  
Tun-Cheng Chien
Keyword(s):  
Reaction Mechanism ◽  
Bond Formation ◽  
Oxidative Cyclization ◽  
Nonheme Iron

scholarly journals Azurin as a Protein Scaffold for a Low-coordinate Nonheme Iron Site with a Small-molecule Binding Pocket

2012 ◽  
Vol 134 (48) ◽  
pp. 19746-19757 ◽  
Author(s):  
Matthew P. McLaughlin ◽  
Marius Retegan ◽  
Eckhard Bill ◽  
Thomas M. Payne ◽  
Hannah S. Shafaat ◽  
...  
Keyword(s):  
Small Molecule ◽  
Binding Pocket ◽  
Nonheme Iron ◽  
Iron Site ◽  
Protein Scaffold

Site of action of nonheme iron in the malate (flavine adenine dinucleotide) pathway of Mycobacterium phlei

1976 ◽  
Vol 22 (7) ◽  
pp. 1054-1057 ◽  
Author(s):  
A. K. Tyagi ◽  
T. L. Prasada Reddy ◽  
T. A. Venkitasubramanian
Keyword(s):  
Electron Transport ◽  
Ultraviolet Light ◽  
Nonheme Iron ◽  
Paramagnetic Resonance ◽  
Iron Protein ◽  
Mycobacterium Phlei ◽  
Diphenyl Tetrazolium Bromide ◽  
Electron Paramagnetic ◽  
Soluble Components ◽  
Malate Oxidation

Irradiation with ultraviolet light (360 nm) of cell-free extracts, electron-transport particles, and soluble components from Mycobacterium phlei resulted in the loss of malate oxidation by the flavine adenine dinucleotide pathway both in cell-free extracts and reconstituted systems. Addition of vitamin K1 restored the loss to the extent of 14% and 11% in cell-free extracts and reconstituted systems respectively. Electron-transport particles from M. phlei upon reduction with malate exhibited electron-paramagnetic resonance signals at g = 2.002 and 1.94, characteristic of napthosemiquinone and nonheme iron protein, respectively. Upon irradiating the particles with ultraviolet light (360 nm) these signals were not observed. Particulate flavine-adenine-dinucleotide-dependent malate dehydrogenase (EC 1.1.1.37) of M. phlei assayed by the 3-(4,5-dimethylthiazolyl-2)-2,5-diphenyl tetrazolium bromide and phenazine methosulfate–2,6-dichlorophenolindophenol systems, which trap electrons at cytochrome c and at the flavine level respectively, was inhibited by o-phenanthroline. These observations suggest that nonheme iron protein is sensitive to ultraviolet light (360 nm) and participates before or in combination with flavine in the malate (flavine adenine dinucleotide) pathway of M. phlei.

Sign in / Sign up

Export Citation Format

Share Document