B. Howes

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Surface Engineering of Gold Nanorods for Cytochrome c Bioconjugation: An Effective Strategy To Preserve the Protein Structure

M. L. Curri, R. Comparelli, A. Agostiano, 2018, ACS omega.

The Met80Ala and Tyr67His/Met80Ala mutants of human cytochrome c shed light on the reciprocal role of Met80 and Tyr67 in regulating ligand access into the heme pocket.

P. Mariottini, M. Coletta, M. Cervelli, 2017, Journal of inorganic biochemistry.

Ibuprofen induces an allosteric conformational transition in the heme complex of human serum albumin with significant effects on heme ligation.

P. Ascenzi, B. Howes, G. Smulevich, 2008, Journal of the American Chemical Society.

Structural determinants of ligand binding in truncated hemoglobins: Resonance Raman spectroscopy of the native states and their carbon monoxide and hydroxide complexes

B. Howes, G. Smulevich, D. Coppola, 2018, Biopolymers.

Unravelling the Non-Native Low-Spin State of the Cytochrome c-Cardiolipin Complex: Evidence of the Formation of a His-Ligated Species Only.

M. Piro, R. Pogni, M. C. Baratto, 2017, Biochemistry.

Interactions between the Photosystem II Subunit PsbS and Xanthophylls Studied in Vivo and in Vitro*

R. Bassi, B. Howes, G. Smulevich, 2008, Journal of Biological Chemistry.

Internal binding of halogenated phenols in dehaloperoxidase-hemoglobin inhibits peroxidase function.

Michael F. Davis, S. Franzen, B. Howes, 2010, Biophysical journal.

Spectroscopic and kinetic properties of the horseradish peroxidase mutant T171S

N. Brissett, Andrew T. Smith, B. Howes, 2005, The FEBS journal.

The Critical Role of the Proximal Calcium Ion in the Structural Properties of Horseradish Peroxidase*

B. Howes, G. Smulevich, L. Raimondi, 2001, The Journal of Biological Chemistry.

Study of manganese binding to the ferroxidase centre of human H-type ferritin.

E. Chiancone, A. Ilari, A. Fiorillo, 2018, Journal of inorganic biochemistry.

Interplay of the H-bond donor-acceptor role of the distal residues in hydroxyl ligand stabilization of Thermobifida fusca truncated hemoglobin.

Juan P. Bustamante, D. Estrin, P. Baiocco, 2014, Biochemistry.

Crystallization, preliminary X-ray diffraction studies and Raman microscopy of the major haemoglobin from the sub-Antarctic fish Eleginops maclovinus in the carbomonoxy form.

L. Vitagliano, A. Vergara, L. Mazzarella, 2010, Acta crystallographica. Section F, Structural biology and crystallization communications.

Pichia pastoris Fep1 is a [2Fe-2S] protein with a Zn finger that displays an unusual oxygen-dependent role in cluster binding

A. Miele, A. Battistoni, B. Howes, 2016, Scientific Reports.

Coexistence of multiple globin genes conferring protection against nitrosative stress to the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125.

P. Ascenzi, C. Verde, G. di Prisco, 2018, Nitric oxide : biology and chemistry.

Ligand‐ and proton‐linked conformational changes of the ferrous 2/2 hemoglobin of Pseudoalteromonas haloplanktis TAC125

Massimo Coletta, Cinzia Verde, Michael C Marden, 2011, IUBMB life.

Combined crystallographic and spectroscopic analysis of Trematomus bernacchii hemoglobin highlights analogies and differences in the peculiar oxidation pathway of Antarctic fish hemoglobins

L. Vitagliano, A. Vergara, F. Sica, 2009, Biopolymers.

Nitrite dismutase reaction mechanism: kinetic and spectroscopic investigation of the interaction between nitrophorin and nitrite.

W. Lubitz, N. Cox, E. Reijerse, 2015, Journal of the American Chemical Society.

pH-dependence for binding a single nitrite ion to each type-2 copper centre in the copper-containing nitrite reductase of Alcaligenes xylosoxidans.

B. Howes, D. Lowe, R. Eady, 1997, The Biochemical journal.

EPR and electron nuclear double resonance (ENDOR) studies show nitrite binding to the type 2 copper centers of the dissimilatory nitrite reductase of Alcaligenes xylosoxidans (NCIMB 11015).

B. Howes, T. Brüser, D. Lowe, 1994, Biochemistry.

From chlorite dismutase towards HemQ–the role of the proximal H-bonding network in haeme binding

S. Hofbauer, C. Obinger, K. Djinović-Carugo, 2016, Bioscience reports.

Evidence favoring molybdenum-carbon bond formation in xanthine oxidase action: 17Q- and 13C-ENDOR and kinetic studies.

B. Howes, R. Bray, D. Lowe, 1996, Biochemistry.

Probing the non‐native states of Cytochrome c with resonance Raman spectroscopy: A tool for investigating the structure–function relationship

L. Tognaccini, B. Howes, G. Smulevich, 2018 .

Extended cardiolipin anchorage to cytochrome c: a model for protein–mitochondrial membrane binding

C. Bombelli, F. Polticelli, M. Coletta, 2010, JBIC Journal of Biological Inorganic Chemistry.

Rupture of the hydrogen bond linking two Omega-loops induces the molten globule state at neutral pH in cytochrome c.

F. Ascoli, M. Piro, B. Howes, 2003, Biochemistry.

Nanohybrid Assemblies of Porphyrin and Au10 Cluster Nanoparticles

B. Howes, G. Smulevich, M. Trapani, 2019, Nanomaterials.

Proton electron-nuclear double-resonance spectra of molybdenum(V) in different reduced forms of xanthine oxidase.

B. Howes, R. Bray, D. Lowe, 1990, Biochemistry.

Haem-linked interactions in horseradish peroxidase revealed by spectroscopic analysis of the Phe-221-->Met mutant.

A. Smith, B. Howes, G. Smulevich, 2001, The Biochemical journal.

4 Ag ↔2 Eg Transition of Mn4+ in Cs2TiF6: MnF6 2-

N. Manson, B. Howes, C. D. Flint, 1977 .

The influence of pH and anions on the adsorption mechanism of rifampicin on silver colloids

S. Sánchez‐Cortés, J. García-Ramos, L. Guerrini, 2007 .

Formation of two types of low-spin heme in horseradish peroxidase isoenzyme A2 at low temperature

B. Howes, G. Smulevich, M. Marzocchi, 2000, JBIC Journal of Biological Inorganic Chemistry.

ATP regulation of the ligand-binding properties in temperate and cold-adapted haemoglobins. X-ray structure and ligand-binding kinetics in the sub-Antarctic fish Eleginops maclovinus.

L. Vitagliano, A. Vergara, L. Mazzarella, 2012, Molecular bioSystems.

Mössbauer and optical spectra of biotite: A case for Fe2+−Fe3+ Interactions

B. Howes, G. Smith, Z. Hasan, 1980 .

Mossbauer and X-ray diffraction studies of M1-xFex(PyNO)6(ClO4)2 (M=Zn, Mg)

B. Howes, D. Price, D. Creagh, 1988 .

An unusual temperature dependence of the EPR parameters of copper(II) and oxovanadium(IV) bis(acetylacetonate) complexes

R. Basosi, R. Pogni, B. Howes, 1999 .

Anatomy of an iron-sulfur cluster scaffold protein: Understanding the determinants of [2Fe-2S] cluster stability on IscU.

A. Pastore, B. Howes, G. Smulevich, 2015, Biochimica et biophysica acta.

13C-ENDOR Studies of the Inhibited Species of Xanthine Oxidase: The First Direct Evidence for a Molybdenum-Carbon Bond in a Biological System

B. Howes, R. Bray, D. Lowe, 1994 .

31P ENDOR studies of xanthine oxidase: coupling of phosphorus of the pterin cofactor to molybdenum (V).

B. Howes, R. Bray, D. Lowe, 1991, Biochemistry.

Recent studies on xanthine oxidase and related enzymes.

J. Whittle, B. Howes, J. Burke, 1996, Biochemical Society transactions.

Biological Polynuclear Clusters Coupled by Magnetic Interactions: From the Point Dipole Approximation to a Local Spin Model

B. Guigliarelli, P. Bertrand, B. Howes, 1994 .

The Role of CyaY in Iron Sulfur Cluster Assembly on the E. coli IscU Scaffold Protein

A. Pastore, B. Howes, G. Smulevich, 2011, PloS one.

Characterisation of some magnetic and magnetoelectric properties of ferroelectric Pb(Fe1/2Nb1/2)O3

P. Fischer, M. Pelizzone, J. Rivera, 1984 .

Mössbauer relaxation spectra of an Ising pseudo-doublet: Influence of the off-diagonal hyperfine coupling

B. Howes, D. Price, 1985 .

Iron spin orientation in a competing anisotropy system: Fe1-xCoxCl2

M. Wiltshire, B. Howes, D. Price, 1984 .

Magnetoelastic coupling at Fe2+ ions in antiferromagnetic CoCl2

M. Wiltshire, B. Howes, D. Price, 1984 .

Benzohydroxamic Acid−Peroxidase Complexes: Spectroscopic Characterization of a Novel Heme Spin Species

B. Howes, G. Smulevich, A. Feis, 2000 .

Observation of S = 2 EPR signals from ferrous iron-thiolate complexes. Relevance to rubredoxin-type sites in proteins

B. Howes, M. Werth, D. Kurtz, 1989 .

Structural flexibility of the heme cavity in the cold‐adapted truncated hemoglobin from the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125

Juan P. Bustamante, Leonardo Boechi, Alessandra Pesce, 2015, The FEBS journal.

Effect of low temperature on soybean peroxidase: spectroscopic characterization of the quantum-mechanically admixed spin state.

B. Howes, M. Marzocchi, A. Feis, 2000, Journal of inorganic biochemistry.

The quantum mixed-spin heme state of barley peroxidase: A paradigm for class III peroxidases.

K. Welinder, J. Shelnutt, B. Howes, 1999, Biophysical journal.

Fifteen years of Raman spectroscopy of engineered heme containing peroxidases: what have we learned?

B. Howes, G. Smulevich, A. Feis, 2005, Accounts of chemical research.

The quantum mechanically mixed-spin state in a non-symbiotic plant hemoglobin: the effect of distal mutation on AHb1 from Arabidopsis thaliana.

B. Howes, G. Smulevich, E. Droghetti, 2007, Journal of inorganic biochemistry.

Mutation of residues critical for benzohydroxamic acid binding to horseradish peroxidase isoenzyme C.

H. Heering, A. Smith, B. Howes, 2001, Biopolymers.

Resonance Raman and electronic absorption spectra of horseradish peroxidase isozyme A2: evidence for a quantum‐mixed spin species

B. Howes, G. Smulevich, A. Feis, 1998 .

Mutation of distal residues of horseradish peroxidase: influence on substrate binding and cavity properties.

A. Smith, B. Howes, G. Smulevich, 1997, Biochemistry.

Insights into the anomalous heme pocket of rainbow trout myoglobin.

A. Fago, B. Howes, G. Smulevich, 2012, Journal of inorganic biochemistry.

New insights into the role of distal histidine flexibility in ligand stabilization of dehaloperoxidase-hemoglobin from Amphitrite ornata.

S. Franzen, B. Howes, G. Smulevich, 2010, Biochemistry.

Oxygen-Linked S-Nitrosation in Fish Myoglobins: A Cysteine-Specific Tertiary Allosteric Effect

A. Gow, A. Fago, B. Howes, 2014, PloS one.

Bridging Theory and Experiment to Address Structural Properties of Truncated Haemoglobins: Insights from Thermobifida fusca HbO.

A. Boffi, B. Howes, G. Smulevich, 2015, Advances in microbial physiology.

Structure-Function Relationships Among Heme Peroxidases: New Insights from Electronic Absorption, Resonance Raman and Multifrequency Electron Paramagnetic Resonance Spectroscopies

A. Ivancich, B. Howes, A. Feis, 2010 .

The peculiar heme pocket of the 2/2 hemoglobin of cold-adapted Pseudoalteromonas haloplanktis TAC125

M. Martí, D. Estrin, M. Coletta, 2011, JBIC Journal of Biological Inorganic Chemistry.

Resonance Raman Characterisation of the His42Leu Mutant of Horseradish Peroxidase

Andrew T. Smith, B. Howes, G. Smulevich, 1995 .

H-bonding networks of the distal residues and water molecules in the active site of Thermobifida fusca hemoglobin.

Juan P. Bustamante, D. Estrin, A. Boffi, 2013, Biochimica et biophysica acta.

Calcium depletion of horseradish peroxidase generates a quantum mechanical mixed-spin heme state

B. Howes, G. Smulevich, A. Feis, 1999 .

Class III heme-containing peroxidases: evidence for a quantum-admixed spin state

B. Howes, G. Smulevich, M. Marzocchi, 1999 .

Occurrence and formation of endogenous histidine hexa‐coordination in cold‐adapted hemoglobins

A. Vergara, L. Mazzarella, C. Verde, 2011, IUBMB life.

Structure and function of the Gondwanian hemoglobin of Pseudaphritis urvillii, a primitive notothenioid fish of temperate latitudes

C. Verde, G. di Prisco, M. D. De Rosa, 2004, Protein science : a publication of the Protein Society.

Role of lysines in cytochrome c-cardiolipin interaction.

F. Polticelli, M. Coletta, M. Piro, 2013, Biochemistry.

Nitrogenase of Klebsiella pneumoniae: electron nuclear double resonance (ENDOR) studies on the substrate reduction site.

K. Fisher, B. Howes, D. Lowe, 1994, Biochemical Journal.

The key role played by charge in the interaction of cytochrome c with cardiolipin

P. Ascenzi, F. Polticelli, M. Coletta, 2016, JBIC Journal of Biological Inorganic Chemistry.

Structure-function relationships in human cytochrome c: The role of tyrosine 67.

P. Mariottini, M. Coletta, M. Cervelli, 2016, Journal of inorganic biochemistry.

Anion concentration modulates the conformation and stability of the molten globule of cytochrome c

M. Coletta, B. Howes, G. Smulevich, 2003, JBIC Journal of Biological Inorganic Chemistry.

The 40s Ω-loop plays a critical role in the stability and the alkaline conformational transition of cytochrome c

F. Ascoli, B. Howes, G. Smulevich, 2004, JBIC Journal of Biological Inorganic Chemistry.

Addition of sodium ascorbate to extend the shelf-life of tuna meat fish: A risk or a benefit for consumers?

B. Howes, G. Smulevich, Lisa Milazzo, 2019, Journal of inorganic biochemistry.

ATP specifically drives refolding of non‐native conformations of cytochrome c

F. Polticelli, F. Ascoli, G. Mei, 2005, Protein science : a publication of the Protein Society.

Insights into the role of the histidines in the structure and stability of cytochrome c

F. Ascoli, G. Mei, M. Piro, 2005, JBIC Journal of Biological Inorganic Chemistry.

Surface‐enhanced resonance Raman spectroscopy of rifamycins on silver nanoparticles: insight into their adsorption mechanisms

B. Howes, G. Smulevich, M. Marzocchi, 2006 .

Ibuprofen induces an allosteric conformational transition in the heme complex of human serum albumin with significant effects on heme ligation.

P. Ascenzi, B. Howes, G. Smulevich, 2008, Journal of the American Chemical Society.

The Met80Ala and Tyr67His/Met80Ala mutants of human cytochrome c shed light on the reciprocal role of Met80 and Tyr67 in regulating ligand access into the heme pocket.

P. Mariottini, M. Coletta, M. Cervelli, 2017, Journal of inorganic biochemistry.

Spectroscopic and crystallographic characterization of a tetrameric hemoglobin oxidation reveals structural features of the functional intermediate relaxed/tense state.

L. Vitagliano, A. Vergara, L. Mazzarella, 2008, Journal of the American Chemical Society.