Crystal Structure of Manganese Catalase from Lactobacillus plantarum

Barynin, V.V.; Whittaker, Mei M.; Antonyuk, S.V.; Lamzin, Victor S.; Harrison, Pauline M.; Artymiuk, Peter J.; Whittaker, James W.

doi:10.1016/s0969-2126(01)00628-1

Cited by 323 publications

(328 citation statements)

References 64 publications

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“…Only three such examples of redox-active polynuclear Mn enzymes are known: Mn-catalase that disproportionates hydrogen peroxide [23][24][25][26]; a Mn form of ribonucleotide reductase (Mn-RNR) [27,28]; and, arguably the most recognized Mn-dependent enzyme, the photosynthetic core of green plants, algae, and certain cyanobacteria termed photosystem II (PSII) [29,30]. Through a series of photoinitiated electron transfer events, oxidizing equivalents are stored on the tetranuclear Mn core of PSII -the oxygen-evolving complex (OEC) -which then extracts four electrons (and four protons) from two substrate water molecules to yield molecular oxygen.…”

Section: Mn-containing Biological Systemsmentioning

confidence: 99%

Multifrequency pulsed EPR studies of biologically relevant manganese(II) complexes

et al. 2007

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Electron paramagnetic resonance studies at multiple frequencies (MF EPR) can provide detailed electronic structure descriptions of unpaired electrons in organic radicals, inorganic complexes, and metalloenzymes. Analysis of these properties aids in the assignment of the chemical environment surrounding the paramagnet and provides mechanistic insight into the chemical reactions in which these systems take part. Herein, we present results from pulsed EPR studies performed at three different frequencies (9, 31, and 130 GHz) on [Mn(II)(H 2 O) 6 ] 2+ , Mn(II) adducts with the nucleotides ATP and GMP, and the Mn(II)-bound form of the hammerhead ribozyme (MnHH). Through line shape analysis and interpretation of the zero-field splitting values derived from successful simulations of the corresponding continuous-wave and field-swept echodetected spectra, these data are used to exemplify the ability of the MF EPR approach in distinguishing the nature of the first ligand sphere. A survey of recent results from pulsed EPR, as well as pulsed electron-nuclear double resonance and electron spin echo envelope modulation spectroscopic studies applied to Mn(II)-dependent systems, is also presented. Mn-Containing Biological SystemsManganese operates as a cofactor in numerous proteins, serving both catalytic and structural roles [1][2][3][4]. Many Mn-dependent enzymes take advantage o f the rich redox chemistry available to the metal, accessing the +2, +3, +4, and perhaps even the +5 oxidation states during their turnover. For example, Mn-superoxide dismutase (MnSOD), which detoxifies the cell of the superoxide radical , cycles between the Mn(II) and Mn(III) oxidation states via the ping-pong type mechanism shown below [5][6][7][8][9].(1a) (1b) Other examples of such mononuclear redox-active enzymes include the manganese peroxidase responsible for lignin degradation by white-rot fungus [10][11][12]; a unique Mndependent form of lipoxygenase [13][14][15][16]; oxalate decarboxylase [17,18]; as well as an extradiol catechol dioxygenase [19][20][21]. NIH-PA Author ManuscriptNIH-PA Author Manuscript NIH-PA Author ManuscriptIn order to help minimize kinetic and thermodynamic penalties associated with electron transfer events and the execution of chemical reactions, two or more metal centers can be coupled together to provide active sites capable of conducting multiple electrons while still operating within a physiologically accessible range of reduction potentials [22]. Only three such examples of redox-active polynuclear Mn enzymes are known: Mn-catalase that disproportionates hydrogen peroxide [23][24][25][26]; a Mn form of ribonucleotide reductase (Mn-RNR) [27,28]; and, arguably the most recognized Mn-dependent enzyme, the photosynthetic core of green plants, algae, and certain cyanobacteria termed photosystem II (PSII) [29,30]. Through a series of photoinitiated electron transfer events, oxidizing equivalents are stored on the tetranuclear Mn core of PSII -the oxygen-evolving complex (OEC) -which then extracts four electr...

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Section: Mn-containing Biological Systemsmentioning

confidence: 99%

Multifrequency pulsed EPR studies of biologically relevant manganese(II) complexes

et al. 2007

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“…Although the exact chemistry of the scavenging has not been determined, the mechanism is thought to involve manganese ions cycling between the Mn 2ϩ and Mn 3ϩ states (2,3,24,45). In its enzymatic capacity, manganese also aids in oxidative stress defense by acting as the essential cofactor in dedicated ROS-scavenging enzymes such as manganese-containing superoxide dismutases and catalases (5,40).…”

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Disruption of sitA Compromises Sinorhizobium meliloti for Manganese Uptake Required for Protection against Oxidative Stress

Davies

Walker

2007

J Bacteriol

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During the initial stages of symbiosis with the host plant Medicago sativa, Sinorhizobium meliloti must overcome an oxidative burst produced by the plant in order for proper symbiotic development to continue. While identifying mutants defective in symbiosis and oxidative stress defense, we isolated a mutant with a transposon insertion mutation of sitA, which encodes the periplasmic binding protein of the putative iron/ manganese ABC transporter SitABCD. Disruption of sitA causes elevated sensitivity to the reactive oxygen species hydrogen peroxide and superoxide. Disruption of sitA leads to elevated catalase activity and a severe decrease in superoxide dismutase B (SodB) activity and protein level. The decrease in SodB level strongly correlates with the superoxide sensitivity of the sitA mutant. We demonstrate that all free-living phenotypes of the sitA mutant can be rescued by the addition of exogenous manganese but not iron, a result that strongly implies that SitABCD plays an important role in manganese uptake in S. meliloti.

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“…This exploitation of metals is mainly enabled by incorporating them into proteins in various forms. An important class of metal proteins are those that contain dinuclear metal (or dimetal) centers at their active sites (1)(2)(3)(4). A common feature of this functionally diverse family is that each dimetal center is embedded in a bundle of four or more helices in a way that enables the binding of dioxygen and/or hydrogen peroxide.…”

mentioning

confidence: 99%

Insights into the Effects on Metal Binding of the Systematic Substitution of Five Key Glutamate Ligands in the Ferritin of Escherichia coli

Stillman

Connolly

Latimer

et al. 2003

Journal of Biological Chemistry

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Living organisms take advantage of the catalytic and redox properties of metals to drive a wide range of vital biological processes. This exploitation of metals is mainly enabled by incorporating them into proteins in various forms. An important class of metal proteins are those that contain dinuclear metal (or dimetal) centers at their active sites (1-4). A common feature of this functionally diverse family is that each dimetal center is embedded in a bundle of four or more helices in a way that enables the binding of dioxygen and/or hydrogen peroxide. With the exception of the dioxygen carrier hemerythrin, in which the metal ligands are found in the motifs HXXXE and HXXXXD, known dimetal centers have either one or two ligand sets within the motif EXXH. Each EXXH motif is located in a separate helix with the Glu residue acting as a bridging ligand between iron atoms, often together with either a second Glu (within a second EXXH motif) or one or more H 2 O, OH Ϫ , or O 2Ϫ

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Crystal Structure of Manganese Catalase from Lactobacillus plantarum

Cited by 323 publications

References 64 publications

Multifrequency pulsed EPR studies of biologically relevant manganese(II) complexes

Multifrequency pulsed EPR studies of biologically relevant manganese(II) complexes

Disruption of sitA Compromises Sinorhizobium meliloti for Manganese Uptake Required for Protection against Oxidative Stress

Insights into the Effects on Metal Binding of the Systematic Substitution of Five Key Glutamate Ligands in the Ferritin of Escherichia coli

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