Abstract
1H NMR spectra at 200-and 600-MHz of manganese peroxidase from Phanerochaete chrysosporium and of its cyanide derivative are reported. The spectrum of the native protein is very similar to that of other peroxidases. The assignment of the spectrum of the cyanide derivative has been performed through ID NOE, 2D NOESY, and COSY experiments. This protein is very similar to lignin peroxidase, the only meaningful difference being the shift of H52 of the proximal histidine. The spectra of the cyanide derivative of these two proteins are compared with those of horseradish peroxidase and cytochrome c peroxidase. The shift pattern of the protons of the proximal histidine is discussed relative to the structural properties which affect the Fe3+/Fe2+ redox potential.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 10009-10017 |
| Number of pages | 9 |
| Journal | Biochemistry |
| Volume | 31 |
| Issue number | 41 |
| DOIs | |
| State | Published - Feb 1 1992 |
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All Science Journal Classification (ASJC) codes
- Biochemistry
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1H NMR Investigation of Manganese Peroxidase from Phanerochaete chrysosporium. A Comparison with Other Peroxidases. / Banci, Lucia; Bertini, Ivano; Turano, Paola; Pease, Elizabeth A.; Tien, Ming.
In: Biochemistry, Vol. 31, No. 41, 01.02.1992, p. 10009-10017.Research output: Contribution to journal › Article
TY - JOUR
T1 - 1H NMR Investigation of Manganese Peroxidase from Phanerochaete chrysosporium. A Comparison with Other Peroxidases
AU - Banci, Lucia
AU - Bertini, Ivano
AU - Turano, Paola
AU - Pease, Elizabeth A.
AU - Tien, Ming
PY - 1992/2/1
Y1 - 1992/2/1
N2 - 1H NMR spectra at 200-and 600-MHz of manganese peroxidase from Phanerochaete chrysosporium and of its cyanide derivative are reported. The spectrum of the native protein is very similar to that of other peroxidases. The assignment of the spectrum of the cyanide derivative has been performed through ID NOE, 2D NOESY, and COSY experiments. This protein is very similar to lignin peroxidase, the only meaningful difference being the shift of H52 of the proximal histidine. The spectra of the cyanide derivative of these two proteins are compared with those of horseradish peroxidase and cytochrome c peroxidase. The shift pattern of the protons of the proximal histidine is discussed relative to the structural properties which affect the Fe3+/Fe2+ redox potential.
AB - 1H NMR spectra at 200-and 600-MHz of manganese peroxidase from Phanerochaete chrysosporium and of its cyanide derivative are reported. The spectrum of the native protein is very similar to that of other peroxidases. The assignment of the spectrum of the cyanide derivative has been performed through ID NOE, 2D NOESY, and COSY experiments. This protein is very similar to lignin peroxidase, the only meaningful difference being the shift of H52 of the proximal histidine. The spectra of the cyanide derivative of these two proteins are compared with those of horseradish peroxidase and cytochrome c peroxidase. The shift pattern of the protons of the proximal histidine is discussed relative to the structural properties which affect the Fe3+/Fe2+ redox potential.
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UR - http://www.scopus.com/inward/citedby.url?scp=0026611621&partnerID=8YFLogxK
U2 - 10.1021/bi00156a021
DO - 10.1021/bi00156a021
M3 - Article
C2 - 1327129
AN - SCOPUS:0026611621
VL - 31
SP - 10009
EP - 10017
JO - Biochemistry
JF - Biochemistry
SN - 0006-2960
IS - 41
ER -