✦ LIBER ✦

Q-band splitting in the spectra of heme proteins

✍ Scribed by Cowan, J. A.; Gray, Harry B.

Book ID: 118276845
Publisher: American Chemical Society
Year: 1989
Tongue: English
Weight: 378 KB
Volume: 28
Category: Article
ISSN: 0020-1669
DOI: 10.1021/ic00324a026

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Electronic and Vibronic Contributions to

Electronic and Vibronic Contributions to the Band Splitting in Optical Spectra of Heme Proteins

✍ Schweitzer-Stenner, Reinhard; Bigman, Dan 📂 Article 📅 2001 🏛 American Chemical Society 🌐 English ⚖ 146 KB

Temperature dependence of Q-band electro

Temperature dependence of Q-band electron paramagnetic resonance spectra of nitrosyl heme proteins

✍ Flores, M.; Wajnberg, E.; Bemski, G. 📂 Article 📅 1997 🏛 Biophysical Society 🌐 English ⚖ 405 KB

Spectral Splitting in the α ( Q 0,0 ) Ab

Spectral Splitting in the α ( Q 0,0 ) Absorption Band of Ferrous Cytochrome c and Other Heme Proteins †

✍ Reddy, K. S.; Angiolillo, P. J.; Wright, W. W.; Laberge, M.; Vanderkooi, J. M. 📂 Article 📅 1996 🏛 American Chemical Society 🌐 English ⚖ 425 KB

Correct interpretation of heme protein s

Correct interpretation of heme protein spectra allows distinguishing between the heme and the protein dynamics

✍ Solomon S. Stavrov 📂 Article 📅 2004 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 67 KB 👁 1 views

## Abstract It is shown by using the vibronic approach that the iron displacement out of the porphyrin plane in deoxyheme proteins intermixes the porphyrin π and axial iron–histidine σ electronic subsystems. This intermixing explains the substantial coupling of the iron–histidine vibration to the h

The impact of altered protein-heme inter

The impact of altered protein-heme interactions on the resonance Raman spectra of heme proteins. Studies of heme rotational disorder

✍ Freeborn Rwere; Piotr J. Mak; James R. Kincaid 📂 Article 📅 2008 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 180 KB 👁 2 views

## Abstract Heme proteins that have been reconstituted with certain hemins may contain substantial fractions of a minor component in which the orientation of the heme in the folded pocket differs from the major (“native”) conformation by a 180° rotation about the α‐γ meso axis. In fact, this minor

Thermal broadening of the Soret band in

Thermal broadening of the Soret band in heme complexes and in heme-proteins: role of iron dynamics

✍ Maurizio Leone; Antonio Cupane; Valeria Militello; Lorenzo Cordone 📂 Article 📅 1994 🏛 Springer 🌐 English ⚖ 402 KB

We report the thermal broadening of the Soret band in heme-CO, heme-OH and protoporphyrin IX in the temperature range 300-20 K. For protoporphyrin IX the temperature dependent Gaussian line broadening follows the behavior predicted by the harmonic approximation in the entire temperature range invest