Biosynthetische anorganische Chemie

Lu, Yi

doi:10.1002/ange.200600168

Cited by 18 publications

(5 citation statements)

References 119 publications

(102 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…[2,5] Furthermore, promiscuous activity was subdivided into three groups, namely 1) condition-, 2) substrate-and 3) catalyticpromiscuity. [6,7] In a recent article entitled How enzymes work, [8] it was stated that the tasks of an enzyme are 1) to bring the reacting species together in a geometry that favours the reaction, 2) to distort the substrate and hence to stabilise one substrate conformation better than the others and to permit it to follow a specific reaction mechanism and 3) to create an inner microenvironments in the protein core leading to altered pK a s of the involved amino acid residues. All these apects contribute to the enzymatic catalysis.…”

Section: Introductionmentioning

confidence: 98%

Ostensible Enzyme Promiscuity: Alkene Cleavage by Peroxidases

Mutti

Lara

Kroutil

et al. 2010

Chemistry A European J

View full text Add to dashboard Cite

Enzyme promiscuity is generally accepted as the ability of an enzyme to catalyse alternate chemical reactions besides the 'natural' one. In this paper peroxidases were shown to catalyse the cleavage of a C=C double bond adjacent to an aromatic moiety for selected substrates at the expense of molecular oxygen at an acidic pH. It was clearly shown that the reaction occurs due to the presence of the enzyme; furthermore, the reactivity was clearly linked to the hemin moiety of the peroxidase. Comparison of the transformations catalysed by peroxidase and by hemin chloride revealed that these two reactions proceed equally fast; additional experiments confirmed that the peptide backbone was not obligatory for the reaction and only a single functional group of the enzyme was required, namely in this case the prosthetic group (hemin). Consequently, we propose to define such a promiscuous activity as 'ostensible enzyme promiscuity'. Thus, we call an activity that is catalysed by an enzyme 'ostensible enzyme promiscuity' if the reactivity can be tracked back to a single catalytic site, which on its own can already perform the reaction equally well in the absence of the peptide backbone.

show abstract

Section: Introductionmentioning

confidence: 98%

Ostensible Enzyme Promiscuity: Alkene Cleavage by Peroxidases

Mutti

Lara

Kroutil

et al. 2010

Chemistry A European J

View full text Add to dashboard Cite

show abstract

“…Recently, excellent examples have been reported on the computational design of functional proteins 1. The design of metalloenzymes has been recognized as being an even more intricate challenge,2a,b since both the requirements of protein structure and metal ion coordination should be fulfilled. Metal ions impart highly tunable redox and catalytic activities to biomolecules, thus rendering them capable of catalyzing important reactions, such as nitrogen fixation, methane hydroxylation, and CO oxidation or insertion, in environmentally benign conditions.…”

Section: Introductionmentioning

confidence: 99%

A Heme–Peptide Metalloenzyme Mimetic with Natural Peroxidase‐Like Activity

Nastri

Lista

Ringhieri

et al. 2011

Chemistry A European J

101

View full text Add to dashboard Cite

Mimicking enzymes with alternative molecules represents an important objective in synthetic biology, aimed to obtain new chemical entities for specific applications. This objective is hampered by the large size and complexity of enzymes. The manipulation of their structures often leads to a reduction of enzyme activity. Herein, we describe the spectroscopic and functional characterization of Fe(III)-mimochrome VI, a 3.5 kDa synthetic heme-protein model, which displays a peroxidase-like catalytic activity. By the use of hydrogen peroxide, Fe(III)-mimochrome VI efficiently catalyzes the oxidation of several substrates, with a typical Michaelis-Menten mechanism and with several multiple turnovers. The catalytic efficiency of Fe(III)-mimochrome VI in the oxidation of 2,2'-azino-di(3-ethyl-benzothiazoline-6-sulfonic acid (ABTS) and guaiacol (k(cat)/K(m)=4417 and 870 mM(-1) s(-1), respectively) is comparable to that of native horseradish peroxidase (HRP, k(cat)/K(m)=5125 and 500 mM(-1) s(-1), respectively). Fe(III)-mimochrome VI also converts phenol to 4- and 2-nitrophenol in the presence of NO(2) (-) and H(2) O(2) in high yields. These results demonstrate that small synthetic peptides can impart high enzyme activities to metal cofactors, and anticipate the possibility of constructing new biocatalysts tailored to specific functions.

show abstract

“…With peptide ligands, an important number of synthetic models have been investigated 11. 12 In contrast, synthesizing a model with conventional organic ligands is far from trivial and remains a real challenge. A major synthetic problem is that such metal–thiolate complexes are generally prone to metal‐reduction processes with concomitant formation of disulfides or, in the presence of dioxygen, to oxygenation at sulfur.…”

Section: Methodsmentioning

confidence: 99%