Dalton transactions : an international journal of inorganic chemistry
Publisher:
Royal Society of Chemistry,
Frequency: Forty eight no. a year, 2006-
Country: England
Language: English
Author(s):
Royal Society of Chemistry (Great Britain)
Start Year:2003 -
ISSN:
1477-9226 (Print)
1477-9234 (Electronic)
1477-9226 (Linking)
1477-9234 (Electronic)
1477-9226 (Linking)
Impact Factor
4
| NLM ID: | 101176026 |
| (OCoLC): | 51500500 |
| Coden: | DTARAF |
| LCCN: | 2003242012 |
| Classification: | W1 DA357 |
Structural and oxygen binding properties of dimeric horse myoglobin. Myoglobin (Mb) stores dioxygen in muscles, and is a fundamental model protein widely used in molecular design. The presence of dimeric Mb has been known for more than forty years, but its structural and oxygen binding properties remain unknown. From an X-ray crystallographic analysis at 1.05 Å resolution, we found that dimeric metMb exhibits a domain-swapped structure with two extended α-helices. Each new long α-helix is formed by the E and F helices and the EF-loop of the original monomer, and as a result the proximal and distal histidines of the heme originate from different protomers. Th...
Formation of a cytochrome c-nitrous oxide reductase complex is obligatory for N2O reduction by Paracoccus pantotrophus. Nitrous oxide reductase (N2OR) catalyses the final step of bacterial denitrification, the two-electron reduction of nitrous oxide (N2O) to dinitrogen (N2). N2OR contains two metal centers; a binuclear copper center, CuA, that serves to receive electrons from soluble donors, and a tetranuclear copper-sulfide center, CuZ, at the active site. Stopped flow experiments at low ionic strengths reveal rapid electron transfer (kobs=150 s-1) between reduced horse heart (HH) cytochrome c and the CuA center in fully oxidized N2OR. When fully reduced N2OR was mixed with oxidized cytochrome c, a similar rat...