Ambient STM and in situ AFM study of nitrite reductase proteins adsorbed on gold and graphite: influence of the substrate on protein interactions.
Trimeric Achromobacter cycloclastes Cu-containing nitrite reductase (CuNIR) proteins adsorbed on gold and graphite have been studied by ambient STM and in situ AFM. STM resolves them individually and in layers, distinguishing the sub-molecular individual units of the trimer. The Cu atoms are not visible to STM. STM shows that individual CuNIR denatures as it adsorbs on Au, although a deformed trimeric shape can be identified in some cases. CuNIR forms disordered layers on gold. On graphite, ordered self-assembled layers of CuNIR have been resolved by in situ AFM and ambient STM forming parallel rows whose separation distance corresponds to the size of one of the units of the trimer, 5nm. Ambient STM can achieve better resolution than in situ AFM in the images of the layers. We observe differences between domains showing the parallel row structure and unstructured parts of the CuNIR layer by in situ phase imaging AFM.
Contera
S Antoranz
SA
Interdisciplinary Nanoscience Centre, Institute of Physics and Astronomy, University of Aarhus, DK 8000, Aarhus C, Denmark. contera@ifa.au.dk
Iwasaki
H
H
Suzuki
S
S
D000327:Adsorption; D000421:Alcaligenes / Q000201:enzymology*; D006046:Gold / Q000737:chemistry*; D006108:Graphite / Q000737:chemistry*; D018625:Microscopy, Atomic Force / Q000379:methods*; D016252:Microscopy, Scanning Tunneling / Q000379:methods*; D009572:Nitrite Reductases / Q000737:chemistry / Q000648:ultrastructure*; D013499:Surface Properties
D006046:Gold; D006108:Graphite; D009572:Nitrite Reductases; C052695:nitrite reductase, copper-containing