De-Orienting Aesthetic Education

Bushnell, Cameron Fae

doi:10.1057/9781137487209.0011

Cited by 1 publication

(2 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In the case of low density monolayer of 1, whose coverage was about one-tenth of that of 1-Au, cyt c gave clear redox wave [4,5]. These results were affected by its structural environment that the heme of cyt c was buried inside of the protein (9]. That is, the association between cyt c and Corn complex was inhibited by the polypeptide chain around the heme, which resulted in the inefficient redox reaction.…”

Section: Methodsmentioning

confidence: 99%

“…All three cytochromes c ( cyt c from horse heart, cyt c 2 from Rhodospiril/um rubrum, and cyt c 553 from Alcaligenes xylosoxidans GIFU 1051) act as an electron transfer protein in a mitochondrial respiratory chain (electron donor: cyt bc 1 complex, electron acceptor: cyt oxidase) [1], photosynthetic bacteria (cyt bc 1 complex, reaction center) [7], and denitrifying bacteria (cyt bc 1 complex, NO reductase) [8], respectively. From the X-ray structure analyses, it has been known that the heme center of cyt c is buried inside of the protein [9] and that of cyt c 2 is located at the protein surface [10]. However, the Electron Transfer Reactions ofC-type Cytochromes with the Self-Assembled Monolayer of the Optically Active Cd 11 Complexes on Au structural information of electron transfer site of cyt cm has not been revealed, except for its axial ligands • (His/Met) [8].…”

mentioning

confidence: 99%

See 1 more Smart Citation

Electron Transfer Reactions of C-type Cytochromes with the Self-Assembled Monolayer of the Optically Active CoIII Complex on Au

Nishijima¹,

Takahashi²,

Inomata³

et al. 2007

Trans. Mat. Res. Soc. Japan

View full text Add to dashboard Cite

In order to obtain the structural information around the active site of three c-type cytochromes ( cyt c from horse heart, cyt c2 from Rhodospirillum rubrum, and cyt cm from Alcaligenes xylosoxidans'G'IFU •051) in aqueous solution, we studied their redox behaviors by use of the densely packed monolayer of the (S)-phenylalanine-containing Corn complex. In the case of cyt c, no redox wave was observed, which agrees with the previous report• that the heme is buried inside of the protein. In contrast, the redox wave of cyt c 2 was clearly observed, which coincides with the fact that the heme positions at the protein surface. Interestingly, in the cyclic voltammogram of cyt c 2 , a splitting of the wave was detected, which was elucidated to be attributable to the protonation/deprotonation ofHis42 imidazole of the protein. Cyt cm, of which the structural information has still not been revealed, gave the redox wave without splitting. In the light of the results of cyt c and cyt c 2 , this redox behavior indicates the existence of two structural characteristics for cyt c 553 : (i) the heme is probably located near the protein surface, and (ii) there is no confoon.atiQnal c;llange caused by the protonation.

show abstract

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%