Peer reviewed research and review articles:

Historical perspective and modern applications of Attenuated Total Reflectance – Fourier Transform Infrared Spectroscopy (ATR-FTIR).
Blum MM, John H.
Drug Test. Anal. 2011 (published online).
http://dx.doi.org/10.1002/dta.374

In vitro and in vivo efficacy of PEGylated Diisopropyl Fluorophosphatase (DFPase).
Melzer M, Heidenreich A, Dorandeu F, Gäb J, Kehe K, Thiermann H, Letzel T, Blum MM.
Drug Test. Anal. 2011 (published online).
http://dx.doi.org/10.1002/dta.363

Review on UV-spectroscopic, chromatographic and electrophoretic methods for the cholinesterase reactivating antidote pralidoxime (2-PAM).
John H, Blum MM.
Drug Test. Anal. 2011 (published online).
http://dx.doi.org/10.1002/dta.327

The DFPase from Loligo Vulgaris in sugar surfactant based bicontinuous microemulsions.
Wellert S, Tiersch B, Koetz J, Richardt A, Lapp A, Holderer O, Gäb J, Blum MM, Schulreich C, Stehle R, Hellweg T.
Eur. Biophys. J. 2011; 40(6):761-774.
http://dx.doi.org/10.1007/s00249-011-0689-0

Formation of pyrophosphate-like adducts from nerve agents sarin, soman and cyclosarin in phosphate buffer: Implications for analytical and toxicological investigations.
Gäb J, John H, Blum MM.
Toxicol. Lett. 2011; 200(1):34-40.
http://dx.doi.org/10.1016/j.toxlet.2010.10.011

Neutron structure and mechanistic studies of diisopropyl fluorophosphatase (DFPase).
Chen JC, Mustyakimov M, Schoenborn B, Langan P, Blum MM.
Acta Crystallogr. Sect. D Biol. Crystallogr. 2010; 66(11):1131-1138.
http://dx.doi.org/10.1107/S0907444910034013

Structural characterization of the catalytic calcium binding site in diisopropyl fluorophosphatase (DFPase) and comparison with related β-propeller enzymes.
Blum MM, Chen JC.
Chem. Biol. Interact. 2010; 187(1-3):373-379.
http://dx.doi.org/10.1016/j.cbi.2010.02.043

X-ray structure of perdeuterated diisopropyl fluorophosphatase (DFPase): Perdeuteration of proteins for neutron diffraction.
Blum MM, Tomanicek S, John H, Hanson L, Rüterjans H, Schoenborn BP, Langan P, Chen JC.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 2010; 66(4):379-385.
http://dx.doi.org/10.1107/S1744309110004318

Stable adducts of nerve agents sarin, soman and cyclosarin with TRIS, TES and related buffer compounds – Characterization by LC-ESI-MS/MS and NMR and implications for analytical chemistry.
Gäb J, John H, Melzer M, Blum MM.
J. Chromatogr. B 2010; 878(17-18):1382-1390.
http://dx.doi.org/10.1016/j.jchromb.2010.01.043

Monitoring the hydrolysis of toxic organophosphonate nerve agents by diisopropyl fluorophosphatase (DFPase) in aqueous buffer and bicontinuous microemulsions with 1H-31P-HSQC NMR spectroscopy.
Gäb J, Melzer M, Kehe K, Wellert S, Hellweg T, Blum MM.
Anal. Bioanal. Chem. 2010;396(3):1213-1221.
http://dx.doi.org/10.1007/s00216-009-3299-2

Reversed Enantioselectivity of Diisopropyl Fluorophosphatase Against Organophohpsorus Nerve Agents by Rational Design.
Melzer M, Chen JC, Heidenreich A, Gäb J, Koller M, Kehe K, Blum MM.
J. Am. Chem. Soc. 2009;131(47):17226-17232.
http://dx.doi.org/10.1021/ja905444g

Highlighted in Nature Chemistry:
Nature Chem. 2010;2(1):4-5.
http://dx.doi.org/10.1038/nchem.487

Rapid determination of hydrogen positions and protonation states of diisopropyl fluorophosphatase by joint neutron and X-ray diffraction refinement.
Blum MM, Mustyakimov M, Rüterjans H, Kehe K, Schoenborn BP, Langan P, Chen JC.
Proc. Natl. Acad. Sci. U S A. 2009 Jan 20;106(3):713-8.
http://dx.doi.org/10.1073/pnas.0807842106

Quantification of hydrolysis of toxic organophosphates and organophosphonates by diisopropyl fluorophosphatase from Loligo vulgaris by in situ Fourier transform infrared spectroscopy.
Gäb J, Melzer M, Kehe K, Richardt A, Blum MM.
Anal. Biochem. 2009; 385(2):187-193.
http://dx.doi.org/10.1016/j.ab.2008.11.012

Inhibitory potency against human acetylcholinesterase and enzymatic hydrolysis of fluorogenic nerve agent mimics by human paraoxonase 1 and squid diisopropyl fluorophosphatase.
Blum MM, Timperley CM, Williams GR, Thiermann H, Worek F.
Biochemistry. 2008; 47(18):5216-24.
http://dx.doi.org/10.1021/bi702222x

Preliminary time-of-flight neutron diffraction study on diisopropyl fluorophosphatase (DFPase) from Loligo vulgaris.
Blum MM, Koglin A, Rüterjans H, Schoenborn B, Langan P, Chen JC.
Acta. Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 2007; 63(1):42-5.
http://dx.doi.org/10.1107/S1744309106052924

Binding of a designed substrate analogue to diisopropyl fluorophosphatase: implications for the phosphotriesterase mechanism.
Blum MM, Löhr F, Richardt A, Rüterjans H, Chen JC.
J. Am. Chem. Soc. 2006; 128(39):12750-7.
http:/dx.doi.org/10.1021/ja061887n

Was wissen Calamari über Sarin? Enzymatische Dekontamination von Nervenkampfstoffen
Richardt A, Blum MM, Mitchell S.
Chemie in unserer Zeit. 2006; 40(4):252-259.
http://dx.doi.org/10.1002/ciuz.200600364

Conformational switches modulate protein interactions in peptide antibiotic synthetases.
Koglin A, Mofid MR, Löhr F, Schäfer B, Rogov VV, Blum MM, Mittag T, Marahiel MA, Bernhard F, Dötsch V.
Science. 2006; 312(5771):273-6.
http:/dx.doi.org/10.1126/science.1122928

Book

Decontamination of Warfare Agents

Together with Dr. Andre Richardt (Armed Forces Scientific Institute for Protection Technologies – NBC Protection in Munster) I am a co-editor and co-author of the book “Decontamination of Warfare Agents – Enzymatic Methods for the Removal of B/C Weapons“, published by Wiley-VCH. The book provides an introduction to the field of chemical and biological weapons and focuses on the use of enzmyes for their detoxification. In addition to a presentation of known enzymes which are active against chemical and biological warfare agents, also technical aspects of their use in the field are discussed. This includes technologies for dispersion as well as carrier systems like micro emulsions. The book concludes with an outlook on future developments.

The book was not only written for specialists in the field of biochemistry. Introductory chapters on proteins or enzyme kinetics also allow access for non-scientists interested in the field.

Table of content:

• History of biological warfare agents
• History of chemical warfare agents
• Monitoring and New Threats of C/B Weapons
• Biological warfare agents
• Chemical warfare agents
• Decontamination of biological warfare agents
• Decontamination of chemical warfare agents
• Introduction to Enzymes
• Hydrolytic Enzymes
• Oxidative Enzyme
• Medical Aspects
• Microemulsions as carriers for decontamination agents
• Immobilisation of enzymes
• The road ahead

ISBN 978-3-5273-1756-1