Redox-active metal(II) complexes of sterically hindered phenolic ligands: Antibacterial activity and reduction of cytochrome c. Part II. Metal(II) complexes of o-diphenol derivatives of thioglycolic acid

Polyhedron ◽  
2011 ◽  
Vol 30 (15) ◽  
pp. 2581-2591 ◽  
Author(s):  
N.V. Loginova ◽  
T.V. Koval’chuk ◽  
Y.V. Faletrov ◽  
Y.S. Halauko ◽  
N.P. Osipovich ◽  
...  
Keyword(s):  
Antibacterial Activity ◽  
Cytochrome C ◽  
Thioglycolic Acid ◽  
Redox Active ◽  
Active Metal ◽  
Sterically Hindered ◽  
Derivatives Of ◽  
Redox Active Metal

Redox-active metal(II) complexes of sterically hindered phenolic ligands: Antibacterial activity and reduction of cytochrome c

Polyhedron ◽  
2010 ◽  
Vol 29 (6) ◽  
pp. 1646-1652 ◽  
Author(s):  
N.V. Loginova ◽  
Y.V. Faletrov ◽  
T.V. Koval’chuk ◽  
N.P. Osipovich ◽  
G.I. Polozov ◽  
...  
Keyword(s):  
Antibacterial Activity ◽  
Cytochrome C ◽  
Redox Active ◽  
Active Metal ◽  
Sterically Hindered ◽  
Redox Active Metal

Analysis of site-directed mutants locates a non-redox-active metal near the active site of cytochrome c oxidase of Rhodobacter sphaeroides

Biochemistry ◽  
1995 ◽  
Vol 34 (23) ◽  
pp. 7586-7592 ◽  
Author(s):  
Jonathan P. Hosler ◽  
Matthew P. Espe ◽  
Yuejun Zhen ◽  
Gerald T. Babcock ◽  
Shelagh Ferguson-Miller
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Rhodobacter Sphaeroides ◽  
Active Site ◽  
Redox Active ◽  
Active Metal ◽  
Redox Active Metal

scholarly journals 3P097 Spectroscopic characterization of the interaction of azide with the redox-active metal sites of fully oxidized cytochrome c oxidase(02. Heme proteins,Poster)

2013 ◽  
Vol 53 (supplement1-2) ◽  
pp. S228
Author(s):  
Masahide Hikita ◽  
Akima Yamamoto ◽  
Tomoko Maeda ◽  
Kyoko Shinzawa-Itoh ◽  
Takashi Ogura ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Heme Proteins ◽  
Spectroscopic Characterization ◽  
Redox Active ◽  
Active Metal ◽  
Redox Active Metal

The emerging molecular structure of the nitrogen cycle: an introduction to the proceedings of the 10th annual N-cycle meeting

2005 ◽  
Vol 33 (1) ◽  
pp. 113-118 ◽  
Author(s):  
C.S. Butler ◽  
D.J. Richardson
Keyword(s):  
Structural Biology ◽  
Nitrogen Cycle ◽  
Reaction Mechanisms ◽  
Spectroscopic Analysis ◽  
Three Dimensional ◽  
Chemical Transformations ◽  
Redox Active ◽  
Active Metal ◽  
Insight Into ◽  
Redox Active Metal

Over the last 10 years, during the lifetime of the nitrogen cycle meetings, structural biology, coupled with spectroscopy, has had a major impact of our understanding enzymology of the nitrogen cycle. The three-dimensional structures for many of the key enzymes have now been resolved and have provided a wealth of information regarding the architecture of redox active metal sites, as well as revealing novel structural folds. Coupled with structure-based spectroscopic analysis, this has led to new insight into the reaction mechanisms of the diverse chemical transformations that together cycle nitrogen in the biosphere. An overview of the some of the key developments in field over the last decade is presented.

scholarly journals Confining the spin between two metal atoms within the carbon cage: redox-active metal–metal bonds in dimetallofullerenes and their stable cation radicals

Nanoscale ◽  
2017 ◽  
Vol 9 (23) ◽  
pp. 7977-7990 ◽  
Author(s):  
Nataliya A. Samoylova ◽  
Stanislav M. Avdoshenko ◽  
Denis S. Krylov ◽  
Hannah R. Thompson ◽  
Amelia C. Kirkhorn ◽  
...  
Keyword(s):  
Carbon Cage ◽  
Cation Radicals ◽  
Metal Atoms ◽  
Redox Active ◽  
Active Metal ◽  
Metal Metal ◽  
Metal Metal Bonds ◽  
Metal Bonds ◽  
Redox Active Metal

Dioxygen-derived radicals in biological systems

1985 ◽  
Vol 311 (1152) ◽  
pp. 605-615 ◽  
Keyword(s):  
Respiratory Burst ◽  
Electrochemical Method ◽  
Culture Medium ◽  
Biological Systems ◽  
Cellular Systems ◽  
Superoxide Ion ◽  
Radical Species ◽  
Redox Active ◽  
Active Metal ◽  
Redox Active Metal

Three instances of the involvement of dioxygen-derived radicals in biological systems are considered. The first concerns the formation of radicals in the haemolytic reactions induced by treatment of erythrocytes by phenylhydrazine, as an example of the so-called ‘oxidant drugs’. The evidence for the formation of phenyl radicals is considered and their origin in the oxidation of phenylhydrazine by a ferryl derivative of haemoglobin postulated. The relevance to the formation of phenylated iron and porphyrin species is described. It is suspected that many instances of oxidative damage to cellular systems result from the coincidence of unsequestered redox-active metal ions (particularly those of iron and copper), reductants, and dioxygen. As an example, the damage to hepatocytes, grown in a culture medium containing cysteine, is described. The formation of radical species derived from dioxygen during the respiratory burst associated with phagocytosis is discussed. A new electrochemical method of detecting the superoxide ion produced during the respiratory burst is described. Particular emphasis is placed on the relation between the production of radical species such as the hydroxyl radical and the superoxide ion, and the extent of phagocytosis.

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