Search

Copyright of Angewandte Chemie is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Using artificial hemes for the reconstruction of natural heme proteins represents a fascinating approach to enhance the bioactivity of the latter. We report the synthesis of various metal 5‐oxaporphyrinium cations as cofactors, and a cobalt 5‐oxaporphyrinium cation was successfully incorporated into the heme‐acquisition protein (HasA) secreted by Pseudomonas aeruginosa. We hypothesize that the oxaporphyrinium cation strongly binds to the HasA‐specific outer membrane receptor (HasR) due to its cationic charge, which prevents the subsequent acquisition of heme. In fact, the reconstructed HasA inhibited the growth of Pseudomonas aeruginosa and even of multidrug‐resistant P. aeruginosa. [ABSTRACT FROM AUTHOR]

Copyright of Angewandte Chemie is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Angewandte Chemie is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Copyright of Angewandte Chemie is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)

Abstract: We report a unique strategy for the development of a H2O2‐dependent cytochrome P450BM3 system, which catalyzes the monooxygenation of non‐native substrates with the assistance of dual‐functional small molecules (DFSMs), such as N‐(ω‐imidazolyl fatty acyl)‐ l‐amino acids. The acyl amino acid group of DFSM is responsible for bounding to enzyme as an anchoring group, while the imidazolyl group plays the role of general acid–base catalyst in the activation of H2O2. This system affords the best peroxygenase activity for the epoxidation of styrene, sulfoxidation of thioanisole, and hydroxylation of ethylbenzene among those P450–H2O2 system previously reported. This work provides the first example of the activation of the normally H2O2‐inert P450s through the introduction of an exogenous small molecule. This approach improves the potential use of P450s in organic synthesis as it avoids the expensive consumption of the reduced nicotinamide cofactor NAD(P)H and its dependent electron transport system. This introduces a promising approach for exploiting enzyme activity and function based on direct chemical intervention in the catalytic process. [ABSTRACT FROM AUTHOR]

Iron(III)-5,15-diphenylporphyrin and several derivatives were accommodated by HasA, a heme acquisition protein secreted by Pseudomonas aeruginosa, despite possessing bulky substituents at the meso position of the porphyrin. Crystal structure analysis revealed that the two phenyl groups at the meso positions of porphyrin extend outside HasA. It was shown that the growth of P. aeruginosa was inhibited in the presence of HasA coordinating the synthetic porphyrins under iron-limiting conditions, and that the structure of the synthetic porphyrins greatly affects the inhibition efficiency. [ABSTRACT FROM AUTHOR]

The selective hydroxylation of benzene to phenol, without the formation of side products resulting from overoxidation, is catalyzed by cytochrome P450BM3 with the assistance of amino acid derivatives as decoy molecules. The catalytic turnover rate and the total turnover number reached 259 min−1 P450BM3−1 and 40 200 P450BM3−1 when N-heptyl- l-proline modified with l-phenylalanine (C7- l-Pro- l-Phe) was used as the decoy molecule. This work shows that amino acid derivatives with a totally different structure from fatty acids can be used as decoy molecules for aromatic hydroxylation by wild-type P450BM3. This method for non-native substrate hydroxylation by wild-type P450BM3 has the potential to expand the utility of P450BM3 for biotransformations. [ABSTRACT FROM AUTHOR]

In their Research Article (e202215706), Hiroshi Sugimoto, Osami Shoji et al. report the crystal structure of cytochrome P450BM3 mimicking the state of the enzyme in the moment preceding epoxidation. Keywords: Asymmetrische Katalyse; Kristallografie; Reaktionsmechanismen; Täuschmoleküle; Zytochrom P450 DE Asymmetrische Katalyse Kristallografie Reaktionsmechanismen Täuschmoleküle Zytochrom P450 1 1 1 03/15/23 20230320 NES 230320 B Enzymes b . [Extracted from the article]

The heme acquisition system A protein secreted by Pseudomonas aeruginosa (HasAp) can capture several synthetic metal complexes other than heme. The crystal structures of HasAp harboring synthetic metal complexes revealed only small perturbation of the overall HasAp structure. An inhibitory effect upon heme acquisition by HasAp bearing synthetic metal complexes was examined by monitoring the growth of Pseudomonas aeruginosa PAO1. HasAp bound to iron-phthalocyanine inhibits heme acquisition in the presence of heme-bound HasAp as an iron source. [ABSTRACT FROM AUTHOR]

Tricks mit Enzymen: Die direkte Hydroxylierung von Benzol zu Phenol wurde durch Wildtyp ‐ P450BM3 in der Gegenwart von perfluorierten Carbonsäuren als Ködermolekülen katalysiert. Der katalytische Umsatz erreichte 120 min−1 pro P450. Die Selektivität für die Phenolbildung war sehr hoch, und Produkte einer Überoxidation wurden nicht nachgewiesen. [ABSTRACT FROM AUTHOR]

Keywords: Cobalt; Heme; Multidrug-Resistant Pseudomonas Aeruginosa; Porphyrinoid; Reconstructed Protein EN Cobalt Heme Multidrug-Resistant Pseudomonas Aeruginosa Porphyrinoid Reconstructed Protein 1 1 1 02/03/22 20220207 NES 220207 B Die violette Wolke b (HasA; ein Häm-Akquisitionsprotein) liefert Cobalt-Oxaporphyrinium (oranges Porphyrin und roter Sauerstoff) zu I Pseudomonas aeruginosa i (grün). Innenrücktitelbild: A Heme-Acquisition Protein Reconstructed with a Cobalt 5-Oxaporphyrinium Cation and Its Growth-Inhibition Activity Toward Multidrug-Resistant Pseudomonas aeruginosa (Angew. Cobalt, Heme, Multidrug-Resistant Pseudomonas Aeruginosa, Porphyrinoid, Reconstructed Protein. [Extracted from the article]

Das Hämbindeprotein HasA aus P. aeruginosa kann Eisen(III)‐5,15‐diphenylporphyrin und mehrere Derivate aufnehmen, auch wenn sie sperrige Substituenten in der meso‐Position des Porphyrins tragen. O. Shoji et al. präsentieren in ihrer Zuschrift auf S. 15481 Kristallstrukturen dieser künstlichen HasAs und weisen nach, dass die wachstumsinhibierende Wirkung gegen P. aeruginosa je nach Struktur des eingefangenen Metallkomplexes variiert. [ABSTRACT FROM AUTHOR]

Hydroxylierung In der Zuschrift auf S. 10460 beschreiben O. Shoji, Y. Watanabe et al. die Verwendung von bestimmten Aminosäurederivaten für die Aktivierung von Cytochrom P450BM3 zur direkten Hydroxylierung von Benzol zu Phenol. [ABSTRACT FROM AUTHOR]