Christine Cavazza

Dr. Christine Cavazza

orcid

Research Focus & Metrics

Academic Career Length

13Years (2014-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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5 February 2020 in Protein Science
Verified
Journal Article
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MAmarila alfano
marila alfano
CCChristine Cavazza
Christine Cavazza
Nickel enzymes, present in archaea, bacteria, plants, and primitive eukaryotes are divided into redox and nonredox enzymes and play key functions in diverse metabolic processes, such as energy metabolism and virulence. They catalyze various reactions by using active sites of diverse complexities, such as mononuclear nickel in Ni‐superoxide dismutase, glyoxylase I and acireductone dioxygenase, dinuclear nickel in urease, heteronuclear metalloclusters in [NiFe]‐carbon monoxide dehydrogenase, acetyl‐CoA decarbonylase/synthase and [NiFe]‐hydrogenase, and even more complex cofactors in methyl‐CoM reductase and lactate racemase. The presence of metalloenzymes in a cell necessitates a tight regulation of metal homeostasis, in order to maintain the appropriate intracellular concentration of nickel while avoiding its toxicity. As well, the biosynthesis and insertion of nickel active sites often require specific and elaborated maturation pathways, allowing the correct metal to be delivered and incorporated into the target enzyme. In this review, the phylogenetic distribution of nickel enzymes will be briefly described. Their tridimensional structures as well as the complexity of their active sites will be discussed. In view of the latest findings on these enzymes, a special focus will be put on the biosynthesis of their active sites and nickel activation of apo‐enzymes.

14 May 2018 in Sustainable Energy & Fuels
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Journal Article
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MAMarila Alfano
Marila Alfano
CCChristine Cavazza
Christine Cavazza
Among the possible renewable energies sources, biomass gasification has been considered one promising alternative to meet the daily growing energy demand. The outcome of this process is a synthetic gas (syngas) mainly composed of carbon monoxide and hydrogen. Syngas can be upgraded by a group of anaerobic micro-organisms, thanks to the biologically mediated water–gas shift (WGS) reaction. In this process, the conversion of CO and H2O into CO2 and H2 is catalyzed by two enzymes: carbon monoxide dehydrogenase (CODH) and hydrogenase. In order to efficiently use micro-organisms as a cost effective and environmentally friendly technology, it is fundamental to deeply understand how this process occurs. In this review paper, an overview on the possible biotechnological uses of the WGS reaction is presented, focusing mainly on the fundamental characterization of the CODH enzyme.

1 January 2015 in Metallomics
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Journal Article
Open access
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HLH. Lebrette
H. Lebrette
EBE. Borezée-Durant
E. Borezée-Durant
LML. Martin
L. Martin
PRP. Richaud
P. Richaud
EEE. Boeri Erba
E. Boeri Erba
CCChristine Cavazza
Christine Cavazza
Staphylococcus aureuspossesses two canonical ABC-importers dedicated to nickel acquisition: the NikABCDE and the CntABCDF systems, active under different growth conditions.

5 December 2017 in Journal of the American Chemical Society
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Journal Article
Closed access
SLSarah Lopez
Sarah Lopez
LRLaurianne Rondot
Laurianne Rondot
CLChloé Leprêtre
Chloé Leprêtre
CMCaroline Marchi-Delapierre
Caroline Marchi-Delapierre
SMStéphane Ménage
Stéphane Ménage
CCChristine Cavazza
Christine Cavazza

1 October 2014 in Structure
Verified
Journal Article
Closed access
HLHugo Lebrette
Hugo Lebrette
CBCéline Brochier-Armanet
Céline Brochier-Armanet
Barbara ZambelliBarbara Zambelli
Barbara Zambelli
HRHilde de Reuse
Hilde de Reuse
EBElise Borezée-Durant
Elise Borezée-Durant
CCChristine Cavazza
Christine Cavazza

27 April 2021 in ACS Catalysis
Verified
Journal Article
Closed access
UCUmberto Contaldo
Umberto Contaldo
BGBruno Guigliarelli
Bruno Guigliarelli
JPJulien Perard
Julien Perard
CRClara Rinaldi
Clara Rinaldi
AGAlan Le Goff
Alan Le Goff
CCChristine Cavazza
Christine Cavazza