Mechanisms of Cysteine‐Lysine Covalent Linkage—The Role of Reactive Oxygen Species and Competition with Disulfide Bonds**

Author:

Ye Jin1,Bazzi Sophia1ORCID,Fritz Tobias1,Tittmann Kai23ORCID,Mata Ricardo A.1ORCID,Uranga Jon1ORCID

Affiliation:

1. Institute for Physical Chemistry Georg-August Universität Göttingen Tammannstraße 6 D-37077 Göttingen Germany

2. Department of Molecular Enzymology Göttingen Center of Molecular Biosciences Georg-August University Göttingen Göttingen Germany

3. Department of Structural Dynamics Max-Planck-Institute for Multidisciplinary Sciences Göttingen Germany

Abstract

AbstractRecently, a new naturally occurring covalent linkage was characterised, involving a cysteine and a lysine, bridged through an oxygen atom. The latter was dubbed as the NOS bond, reflecting the individual atoms involved in this uncommon bond which finds little parallel in lab chemistry. It is found to form under oxidising conditions and is reversible upon addition of reducing agents. Further studies have identified the bond in crystal structures across a variety of systems and organisms, potentially playing an important role in regulation, cellular defense and replication. Not only that, double NOS bonds have been identified and even found to be competitive in relation to the formation of disulfide bonds. This raises several questions about how this exotic bond comes to be, what are the intermediates involved in its formation and how it competes with other pathways of sulfide oxidation. With this objective in mind, we revisited our first proposed mechanism for the reaction with model electronic structure calculations, adding information about the reactivity with alternative reactive oxygen species and other potential competing products of oxidation. We present a network with more than 30 reactions which provides one of the most encompassing pictures for cysteine oxidation pathways to date.

Funder

Deutsche Forschungsgemeinschaft

Publisher

Wiley

Subject

General Medicine

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