Metalloproteins

Abstract

Cover illustrationEnzymes that contain metal atoms (yellow) at their active sites are involved in many biological processes. (Artwork by N. Spencer) METALLOPROTEINS Proteins can catalyse a remarkably wide range of chemical reactions. Yet the main differences among polypeptides are in the side chains of naturally occurring amino acids, which account for only a small proportion of the possible chemical functionality. The diversity of function is instead made possible partly because proteins can incorporate cofactors -such as small organic molecules, single metal atoms or clusters that contain metal and non-metal atoms -into their active sites.Almost half of all enzymes require the presence of a metal atom to function. These 'metalloproteins' have captivated chemists and biochemists, particularly since the 1950s, when the first X-ray crystal structure of a protein, sperm whale myoglobin, indicated the presence of an iron atom. Much is now understood about how metal clusters are assembled, how metal ions or clusters are introduced into target proteins, and which metal ions are commonly found in metalloenzymes. In addition, we are much closer to understanding the mechanisms by which metalloenzymes catalyse such a range of complex chemical reactions. But, despite more than half a century of research by chemists, biochemists and cell biologists, many discoveries remain to be made.The articles in this Insight highlight some of the most exciting current research on metalloproteins, including how enzymes containing complex metal clusters metabolize small gaseous molecules, how proteins containing iron-sulphur clusters are assembled, and how metalloenzymes containing a single metal ion catalyse the halogenation of small organic molecules.We are pleased to acknowledge the financial support of AstraZeneca in producing this Insight. As always, Nature carries sole responsibility for all editorial content and peer review. Joshua Finkelstein, Senior Editor REVIEWS814 Structure-function relationships of anaerobic gas-processing metalloenzymes

DFT investigation of the effect of spin-orbit coupling on the NMR shifts in paramagnetic solids

“…Materials containing paramagnetic centres with unpaired electron spins, such as transition metal (TM) ions, are widely used in the fields of biochemistry [1,2], catalysis [3][4][5], and electrochemistry [6][7][8]. Nuclear Magnetic Resonance (NMR) spectroscopy is a powerful technique for analysing the local structure in paramagnetic solids, as the unpaired electrons of the TM ions induce a paramagnetic shift and shift anisotropy that provide detailed information concerning the structural and chemical environment of the NMR observed centre (OC) [9][10][11][12][13].…”

MetalloPred: A tool for hierarchical prediction of metal ion binding proteins using cluster of neural networks and sequence derived features

“…Metalloproteins have captivated chemists and biochemists, particularly since 1950s, when the first X-ray crystal structure of a protein, sperm whale myoglobin indicated the presence of an iron atom [1]. The metal ion is usually coordinated by nitrogen, oxygen or sulfur atoms belonging to amino acids in the polypeptide chain and/or a macro-cyclic ligand incorporated into the protein [2,3].…”

“…The metal ion is usually coordinated by nitrogen, oxygen or sulfur atoms belonging to amino acids in the polypeptide chain and/or a macro-cyclic ligand incorporated into the protein [2,3]. The presence of the metal ion allows metalloenzymes to perform functions such as redox reactions that cannot be performed by the limited set of functional groups found in amino acids [1]. Metalloproteins play important roles in structural stability and complex formation [4][5][6][7][8], gene expression regulation and alteration [9][10][11][12], DNA processing [13], signaling processes and cellular event [14], transport [11,15,16], metabolism control [15,17], antibody recognition [18] and other biological processes such as cellular respiration, photosynthesis, nitrogen fixation and antioxidant defense [19].…”

Papel de COPT1, COPT2, MTP2 y ZIP6 en el transporte y la homeostasis de metales en Medicago truncatula

“…El cobre y el zinc son cofactores esenciales de enzimas involucradas en múltiples procesos fisiológicos (Finkelstein, 2009). En plantas participan, entre otros procesos, en la fotosíntesis (Yruela, 2013), en la respiración oxidativa (Ravet & Pilon, 2013), la floración (Takahashi et al, 2003), y, en el caso de las leguminosas, en la fijación simbiótica de nitrógeno (Brear et al, 2013;González-Guerrero et al, 2016).…”

“…Copper and zinc are essential cofactors of enzymes involved in multiple physiological processes (Finkelstein, 2009). In plants, they participate in photosynthesis (Yruela, 2013), oxidative respiration (Ravet & Pilon, 2013), flowering (Takahashi et al, 2003), and, in the case of legumes, in symbiotic nitrogen fixation (Brear et al, 2013;González-Guerrero et al, 2016), among others.…”