scholarly journals Spectroscopic Characterization of Active-Site Variants of the PduO-type ATP:Corrinoid Adenosyltransferase from Lactobacillus reuteri: Insights into the Mechanism of Four-Coordinate Co(II)corrinoid Formation

2012 ◽  
Vol 51 (8) ◽  
pp. 4482-4494 ◽  
Author(s):  
Kiyoung Park ◽  
Paola E. Mera ◽  
Jorge C. Escalante-Semerena ◽  
Thomas C. Brunold
Keyword(s):  
Active Site ◽  
Lactobacillus Reuteri ◽  
Spectroscopic Characterization

Replacement of non-heme Fe(II) with Cu(II) in the α-ketoglutarate dependent DNA repair enzyme AlkB: Spectroscopic characterization of the active site

2007 ◽  
Vol 101 (7) ◽  
pp. 1043-1048 ◽  
Author(s):  
Boris Bleijlevens ◽  
Tara Shivarattan ◽  
Barbara Sedgwick ◽  
Stephen E.J. Rigby ◽  
Steve J. Matthews
Keyword(s):  
Dna Repair ◽  
Active Site ◽  
Spectroscopic Characterization ◽  
Repair Enzyme

Cytochrome cbb3 oxidase and bacterial microaerobic metabolism

2002 ◽  
Vol 30 (4) ◽  
pp. 653-658 ◽  
Author(s):  
R. S. Pitcher ◽  
T. Brittain ◽  
N. J. Watmugh
Keyword(s):  
Active Site ◽  
Reduction Potential ◽  
Oxygen Affinity ◽  
Pseudomonas Stutzeri ◽  
Spectroscopic Characterization ◽  
High Oxygen Affinity ◽  
Copper Oxidase ◽  
Reduced State

Cytochrome cbb3 oxidase is a member of the haem-copper oxidase superfamily. It is characterized by its high oxygen affinity, while retaining the ability to pump protons. These attributes are central to its proposed role in bacterial microaerobic metabolism. Recent spectroscopic characterization of both the cytochrome cbb3 oxidase complex from Pseudomonas stutzeri and the dihaem ccoP subunit expressed separately in Escherichia coli has revealed the presence of a low-spin His/His co-ordinated c-type cytochrome. The low midpoint reduction potential of this haem (Em < + 100 mV), together with its unexpected ability to bind CO in the reduced state at the expense of the distal histidine ligand, raises questions about the role of the ccoP subunit in the delivery of electrons to the active site.

Spectroscopic characterization of the trinuclear copper active site in laccase

1989 ◽  
Vol 36 (3-4) ◽  
pp. 245
Author(s):  
J.L. Cole ◽  
E.K. Yang ◽  
P.O. Sandusky ◽  
E.I. Solomon
Keyword(s):  
Active Site ◽  
Spectroscopic Characterization

Resonance Raman Spectroscopic Characterization of the Molybdopterin Active Site of DMSO Reductase

Biochemistry ◽  
1995 ◽  
Vol 34 (9) ◽  
pp. 3032-3039 ◽  
Author(s):  
L. Kilpatrick ◽  
K. V. Rajagopalan ◽  
J. Hilton ◽  
N. R. Bastian ◽  
E. I. Stiefel ◽  
...  
Keyword(s):  
Active Site ◽  
Resonance Raman ◽  
Spectroscopic Characterization ◽  
Dmso Reductase ◽  
Raman Spectroscopic

scholarly journals Atypical Iron-Sulfur Cluster Binding, Redox Activity and Structural Properties of Chlamydomonas reinhardtii Glutaredoxin 2

Antioxidants ◽  
2021 ◽  
Vol 10 (5) ◽  
pp. 803
Author(s):  
Thomas Roret ◽  
Bo Zhang ◽  
Anna Moseler ◽  
Tiphaine Dhalleine ◽  
Xing-Huang Gao ◽  
...  
Keyword(s):  
Chlamydomonas Reinhardtii ◽  
Structural Properties ◽  
Active Site ◽  
Fluorescent Protein ◽  
Spectroscopic Characterization ◽  
Redox Activity ◽  
Structural Factors ◽  
Oxidoreductase Activity ◽  
Iron Sulfur

Glutaredoxins (GRXs) are thioredoxin superfamily members exhibiting thiol-disulfide oxidoreductase activity and/or iron-sulfur (Fe-S) cluster binding capacities. These properties are determined by specific structural factors. In this study, we examined the capacity of the class I Chlamydomonas reinhardtii GRX2 recombinant protein to catalyze both protein glutathionylation and deglutathionylation reactions using a redox sensitive fluorescent protein as a model protein substrate. We observed that the catalytic cysteine of the CPYC active site motif of GRX2 was sufficient for catalyzing both reactions in the presence of glutathione. Unexpectedly, spectroscopic characterization of the protein purified under anaerobiosis showed the presence of a [2Fe-2S] cluster despite having a presumably inadequate active site signature, based on past mutational analyses. The spectroscopic characterization of cysteine mutated variants together with modeling of the Fe–S cluster-bound GRX homodimer from the structure of an apo-GRX2 indicate the existence of an atypical Fe–S cluster environment and ligation mode. Overall, the results further delineate the biochemical and structural properties of conventional GRXs, pointing to the existence of multiple factors more complex than anticipated, sustaining the capacity of these proteins to bind Fe–S clusters.

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