Abstract
Supramolecular mimics of metalloproteins, viz. cytochrome P-450 and ironsulfur proteins are described. The cytochrome P-450 mimic consists of a Mn porphyrin and a Rh complex which are incorporated within a vesicle membrane in water. This system catalyses the reductive activation of molecular oxygen in the epoxidation of alkenes at Mn, with reducing equivalents derived from the simultaneous Rh catalysed oxidation of formate to carbon dioxide. In the mimics for iron-sulfur proteins, iron-sulfur clusters are encapsulated in diphenylglycoluril and cyclotriveratrylene cavitands. The encapsulation by the cavitands modifies the electrochemical parameters, e.g. the redox potential, of the iron-sulfur clusters, in a way that has certain analogies to the effects of encapsulation by the protein in ferredoxins and high-potential iron-sulfur proteins.
| Language | English |
|---|---|
| Pages | 2163-2170 |
| Number of pages | 8 |
| Journal | Pure and Applied Chemistry |
| Volume | 68 |
| Issue number | 11 |
| DOIs | |
| State | Published - 1 Jan 1996 |
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Development of supramolecular metalloprotein mimics. / Feiters, M.C.; Klein Gebbink, R.J.M.; Schenning, A.P.H.J.; van Strijdonck, G.P.F.; Martens, C.F.; Nolte, R.J.M.
In: Pure and Applied Chemistry, Vol. 68, No. 11, 01.01.1996, p. 2163-2170.Research output: Contribution to journal › Article › Academic › peer-review
TY - JOUR
T1 - Development of supramolecular metalloprotein mimics
AU - Feiters,M.C.
AU - Klein Gebbink,R.J.M.
AU - Schenning,A.P.H.J.
AU - van Strijdonck,G.P.F.
AU - Martens,C.F.
AU - Nolte,R.J.M.
PY - 1996/1/1
Y1 - 1996/1/1
N2 - Supramolecular mimics of metalloproteins, viz. cytochrome P-450 and ironsulfur proteins are described. The cytochrome P-450 mimic consists of a Mn porphyrin and a Rh complex which are incorporated within a vesicle membrane in water. This system catalyses the reductive activation of molecular oxygen in the epoxidation of alkenes at Mn, with reducing equivalents derived from the simultaneous Rh catalysed oxidation of formate to carbon dioxide. In the mimics for iron-sulfur proteins, iron-sulfur clusters are encapsulated in diphenylglycoluril and cyclotriveratrylene cavitands. The encapsulation by the cavitands modifies the electrochemical parameters, e.g. the redox potential, of the iron-sulfur clusters, in a way that has certain analogies to the effects of encapsulation by the protein in ferredoxins and high-potential iron-sulfur proteins.
AB - Supramolecular mimics of metalloproteins, viz. cytochrome P-450 and ironsulfur proteins are described. The cytochrome P-450 mimic consists of a Mn porphyrin and a Rh complex which are incorporated within a vesicle membrane in water. This system catalyses the reductive activation of molecular oxygen in the epoxidation of alkenes at Mn, with reducing equivalents derived from the simultaneous Rh catalysed oxidation of formate to carbon dioxide. In the mimics for iron-sulfur proteins, iron-sulfur clusters are encapsulated in diphenylglycoluril and cyclotriveratrylene cavitands. The encapsulation by the cavitands modifies the electrochemical parameters, e.g. the redox potential, of the iron-sulfur clusters, in a way that has certain analogies to the effects of encapsulation by the protein in ferredoxins and high-potential iron-sulfur proteins.
UR - http://www.scopus.com/inward/record.url?scp=0000997493&partnerID=8YFLogxK
U2 - 10.1351/pac199668112163
DO - 10.1351/pac199668112163
M3 - Article
VL - 68
SP - 2163
EP - 2170
JO - Pure and Applied Chemistry
T2 - Pure and Applied Chemistry
JF - Pure and Applied Chemistry
SN - 0033-4545
IS - 11
ER -