And YHK participated within the discussion of the outcomes and writing on the manuscript. All authors read and approved the final manuscript.Fig. 6 Interaction amongst A242D and its surrounding residues: a hydrogen bonding and b charge harge interaction. Numbers aligned with arrows indicate the pKa shift impact on A242DAuthor facts 1 College of Power and Chemical Engineering, UNIST, 50 UNIST-gil, Ulju-gun, Ulsan 44919, Republic of Korea. two Life Ingredient Material Investigation Institute, CJ Company, 42 Gwanggyo-ro, Yeongtong-gu, Suwon-si, Gyeonggi-do, Republic of Korea. Acknowledgements We gratefully acknowledge the MOTIEKEIT (10049675), KCRC (2014M1A8A1049296), KCGRC (2015M3D3A1A01064919), and UNIST Start-Up Grant 2016 for their assistance of this function. We also thank Dr. Youn Min Hye (Korea Institute Power Investigation) for help in performing transient kinetics and Dr. Joo Jeong Chan, Oh Joon Young (Korea Analysis Institute of Chemical Technology) for technical help in enzyme purification. Competing interests The authors declare that they have no competing interests. Availability of supporting information All information generated or analyzed during this study are integrated in this published report and its added files. Consent for publication All authors agree to publication. Funding MOTIEKEIT (10049675), KCRC (2014M1A8A1049296), KCGRC (2015M3D3A1A01064919), UNIST Start-Up Grant 2016. Received: 29 September 2016 Accepted: 9 NovemberFig. 7 Proposed multistep tunneling approach in LRET amongst W171 and Heme by means of W251 and FPham et al. Biotechnol Biofuels (2016) 9:Page 10 ofReferences 1. Tien M, Kirk TK. Lignin-degrading enzyme from the Hymenomycete Phanerochaete chrysosporium Burds. Science. 1983;221:661. 2. Fern dez-Fueyo E, Ruiz-Due s FJ, Mart ez MJ, Romero A, Hammel KE, Medrano FJ, Mart ez AT. Ligninolytic Pentagastrin supplier peroxidase genes within the oyster mushroom genome heterologous expression, molecular structure, catalytic and SB-612111 site stability properties, and lignin-degrading capability. Biotechnol Biofuels. 2014;7(1):two. three. Smith AT, Doyle WA, Dorlet P, Ivancich A. Spectroscopic proof for an engineered, catalytically active Trp radical that creates the exclusive reactivity of lignin peroxidase. Proc Natl Acad Sci USA. 2009;106:16084. 4. Saez-Jimenez V, Baratto MC, Pogni R, Rencoret J, Gutierrez A, Santos JI, Martinez AT, Ruiz-Duenas FJ. Demonstration of lignin-to-peroxidase direct electron transfer: a transient-state kinetics, directed mutagenesis, EPR and NMR study. J Biol Chem. 2015;290:232013. five. Semba Y, Ishida M, Yokobori S, Yamagishi A. Ancestral amino acid substitution improves the thermal stability of recombinant lignin-peroxidase from white-rot fungi, Phanerochaete chrysosporium strain UAMH 3641. Protein Eng Des Sel. 2015;28:2210. 6. Saez-Jimenez V, Fernandez-Fueyo E, Medrano FJ, Romero A, Martinez AT, Ruiz-Duenas FJ. Enhancing the pH-stability of versatile peroxidase by comparative structural evaluation having a naturally-stable manganese peroxidase. PLoS One particular. 2015;ten:e0140984. 7. Pham LTM, Eom MH, Kim YH. Inactivating impact of phenolic unit structures around the biodegradation of lignin by lignin peroxidase from Phanerochaete chrysosporium. Enzyme Microb Technol. 2014;612:484. 8. Doyle WA, Smith AT. Expression of lignin peroxidase H8 in Escherichia coli: folding and activation with the recombinant enzyme with Ca2+ and haem. Biochem J. 1996;315:15. 9. Urban A, Neukirchen S, Jaeger KE. A speedy and efficient technique for sitedirected mutagenesis working with one-step overlap extensio.
