1993
DOI: 10.1016/0014-5793(93)80430-3
|View full text |Cite
|
Sign up to set email alerts
|

Cytochrome d axial ligand of the bd‐type terminal quinol oxidase from Escherichia coli

Abstract: Using various spectroscopic techniques, we studied the structure of the dioxygen reduction site of the bd‐type terminal quinol oxidase in the aerobic respiratory chain of Escherichia coli. Resonance Raman and FT‐IR spectroscopies identified the v(Fe2+‐CO) and v(C‐O) stretching frequencies at 471 and 1980.7 cm−1, respectively, at the cytochrome d center of the dithionite‐reduced CO‐bound enzyme. The CO ligation in the cytochrome bd complex is considerably different from those of the heme‐copper terminal oxidase… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1

Citation Types

2
16
0

Year Published

1994
1994
2013
2013

Publication Types

Select...
7

Relationship

2
5

Authors

Journals

citations
Cited by 14 publications
(18 citation statements)
references
References 40 publications
(22 reference statements)
2
16
0
Order By: Relevance
“…1) (28). Exposure of the air-oxidized O 2 -bound sample to a CO atmosphere caused a shift of the 647 nm peak to 635 nm, consistent with the formation of the cytochrome d (Fe 2ϩ )-CO species (3,4,16). The addition of cyanide to this air-oxidized CO-bound enzyme also caused the characteristic 635 nm band to disappear.…”
Section: Heme B Metal Contents and Optical Extinction Coefficients-mentioning
confidence: 69%
See 3 more Smart Citations
“…1) (28). Exposure of the air-oxidized O 2 -bound sample to a CO atmosphere caused a shift of the 647 nm peak to 635 nm, consistent with the formation of the cytochrome d (Fe 2ϩ )-CO species (3,4,16). The addition of cyanide to this air-oxidized CO-bound enzyme also caused the characteristic 635 nm band to disappear.…”
Section: Heme B Metal Contents and Optical Extinction Coefficients-mentioning
confidence: 69%
“…Fax: 81-7915-8-0189; E-mail: tsubaki@sci.himeji-tech.ac.jp. ments were carried out at X-band (9.23 GHz) microwave frequency with a home-built EPR spectrometer as described previously (16,22) and a Varian E-12 EPR spectrometer equipped with an Oxford flow cryostat (ESR-900). Infrared spectra were recorded at 4°C with a Perkin-Elmer (model 1850) FT-IR spectrophotometer as described previously (24) or a JASCO (model VALOR-III) FT-IR spectrophotometer.…”
Section: Methodsmentioning
confidence: 99%
See 2 more Smart Citations
“…1B). The consensus of recent spectral data from electron paramagnetic resonance (EPR), electron nuclear double resonance (ENDOR), Fouriertransform infra-red spectroscopy (FT-IR) and resonance Raman studies of cytochrome bd is that the proximal ligand is not cysteine or methionine, and that if it is a histidine or strong nitrogenous ligand then the residue is in an unusual environment (Tsubaki et al, 1993;Hirota et al, 1995).…”
Section: Figmentioning
confidence: 99%