Electronic Characterization of the Oxidized State of the Blue Copper Protein Rusticyanin by1H NMR:  Is the Axial Methionine the Dominant Influence for the High Redox Potential?†

Biochemistry ◽  
2001 ◽  
Vol 40 (3) ◽  
pp. 837-846 ◽  
Author(s):  
Antonio Donaire ◽  
Beatriz Jiménez ◽  
José-María Moratal ◽  
John F. Hall ◽  
S. Samar Hasnain
Keyword(s):  
Redox Potential ◽  
Blue Copper Protein ◽  
Blue Copper ◽  
Copper Protein ◽  
Dominant Influence ◽  
High Redox Potential

scholarly journals Isolation and characterization of a blue copper protein from Thiobacillus versutus

1985 ◽  
Vol 153 (1) ◽  
pp. 75-80 ◽  
Author(s):  
Tiny HOUWELINGEN ◽  
Gerard W. CANTERS ◽  
George STOBBELAAR ◽  
Johannis A. DUINE ◽  
Johannes FRANK Jzn ◽  
...  
Keyword(s):  
Blue Copper Protein ◽  
Blue Copper ◽  
Copper Protein ◽  
Isolation And Characterization ◽  
Thiobacillus Versutus

Characterization of a blue-copper protein, auracyanin, of the filamentous anoxygenic phototrophic bacterium Roseiflexus castenholzii

2009 ◽  
Vol 490 (1) ◽  
pp. 57-62 ◽  
Author(s):  
Yusuke Tsukatani ◽  
Nahomi Nakayama ◽  
Keizo Shimada ◽  
Hiroyuki Mino ◽  
Shigeru Itoh ◽  
...  
Keyword(s):  
Blue Copper Protein ◽  
Blue Copper ◽  
Copper Protein ◽  
Phototrophic Bacterium ◽  
Anoxygenic Phototrophic Bacterium

scholarly journals The role of blue copper proteins in the oxidation of methylamine by an obligate methylotroph

1985 ◽  
Vol 228 (3) ◽  
pp. 719-726 ◽  
Author(s):  
S A Lawton ◽  
C Anthony
Keyword(s):  
Absorption Coefficient ◽  
Redox Potential ◽  
Absorption Maximum ◽  
Copper Proteins ◽  
Blue Copper Proteins ◽  
Blue Copper Protein ◽  
Methylamine Dehydrogenase ◽  
Obligate Methylotroph ◽  
Blue Copper ◽  
Copper Protein

Organism 4025, an obligate methylotroph, when grown on methylamine in the presence of a high concentration of copper, contained high concentrations of methylamine dehydrogenase and two blue copper proteins, amicyanin and an azurin-type protein; these were purified to homogeneity and characterized. The methylamine dehydrogenase is a basic protein (pI 8.8) and consists of light and heavy subunits (Mr 14100 and 43000; total Mr 112000). This dehydrogenase differed slightly from other methylamine dehydrogenases in its absorption spectrum and in its lack of thermal stability. Amicyanin, the more abundant blue copper protein, had an Mr of 11500, a midpoint redox potential of 294mV at pH 7.0, and a much lower isoelectric point (pI5.3) than other amicyanins. Its absorption maximum was 620 nm (7-24 nm higher than those of other amicyanins); its absorption coefficient (at 620 nm) was 3.8 mM-1 X cm-1. The ‘azurin’ (6% of the blue copper protein) had an Mr of 12500, a midpoint redox potential of 323 mV and a high isoelectric point (pI 9.4). Its absorption maximum was 620 nm, the absorption coefficient (16 mM-1 X cm-1) at this wavelength being considerably greater than that of any blue copper protein described previously. The partially-purified soluble cytochromes cH and cL were similar to those of other methylotrophs. The interactions of the purified redox proteins were investigated in order to elucidate their role in methylamine oxidation. Methylamine dehydrogenase was able to donate electrons only to amicyanin, the rate of reaction being 2.04 mmol/min per mumol of methylamine dehydrogenase; this is sufficient to account for the rate of respiration in whole bacteria. The blue copper proteins were able to react rapidly with each other and with both the soluble cytochromes c.

Electrochemical and spectral characterization of blue copper protein models

2009 ◽  
Vol 11 (4) ◽  
pp. 878-880 ◽  
Author(s):  
Harmeet Dhillon ◽  
Kavita Sharma ◽  
Rakhee Gehlot ◽  
Sunita Kumbhat
Keyword(s):  
Spectral Characterization ◽  
Blue Copper Protein ◽  
Blue Copper ◽  
Copper Protein ◽  
Protein Models

Blue copper protein analogue: synthesis and characterization of copper complexes of the N2S2 macrocycle 1,8-dithia-4,11-diazacyclotetradecane

2015 ◽  
Vol 44 (46) ◽  
pp. 20200-20206 ◽  
Author(s):  
Tia L. Walker ◽  
Sam Mula ◽  
Wilhelm Malasi ◽  
James T. Engle ◽  
Christopher J. Ziegler ◽  
...  
Keyword(s):  
Crystal Structures ◽  
Copper Complexes ◽  
Spectroscopic Characterization ◽  
Synthesis And Characterization ◽  
Blue Copper Protein ◽  
Blue Copper ◽  
Copper Protein ◽  
X Ray

We report the synthesis, spectroscopic characterization and X-ray crystal structures of CuI/II complexes prepared from the N2S2 macrocycle 1,8-dithia-4,11-diazacyclotetradecane.

Sign in / Sign up

Export Citation Format

Share Document