PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
23634216-1	2013	P450(cam) (CYP101A1) is a bacterial monooxygenase that is known to catalyze the oxidation of camphor, the first committed step in camphor degradation, with simultaneous reduction of oxygen (O2).	Camphor	93-100	calmodulin 3	Homo sapiens	0-9	
23634216-1	2013	P450(cam) (CYP101A1) is a bacterial monooxygenase that is known to catalyze the oxidation of camphor, the first committed step in camphor degradation, with simultaneous reduction of oxygen (O2).	Camphor	130-137	calmodulin 3	Homo sapiens	0-9	
23634216-2	2013	We report that P450(cam) catalysis is controlled by oxygen levels: at high O2 concentration, P450(cam) catalyzes the known oxidation reaction, whereas at low O2 concentration the enzyme catalyzes the reduction of camphor to borneol.	Camphor	213-220	calmodulin 3	Homo sapiens	15-24	
23634216-2	2013	We report that P450(cam) catalysis is controlled by oxygen levels: at high O2 concentration, P450(cam) catalyzes the known oxidation reaction, whereas at low O2 concentration the enzyme catalyzes the reduction of camphor to borneol.	Camphor	213-220	calmodulin 3	Homo sapiens	93-102	
23634216-5	2013	The reduction of camphor and simultaneous oxidation of water are likely catalyzed by the iron-oxo intermediate of P450(cam) , and we present a plausible mechanism that accounts for the 1:1 borneol:H2O2 stoichiometry we observed.	Camphor	17-24	calmodulin 3	Homo sapiens	114-123	
23634216-6	2013	This reaction has an adaptive value to bacteria that express this camphor catabolism pathway, which requires O2, for two reasons: 1) the borneol and H2O2 mixture generated is toxic to other bacteria and 2) borneol down-regulates the expression of P450(cam) and its electron transfer partners.	Camphor	66-73	calmodulin 3	Homo sapiens	247-256	
18513977-1	2008	The two-protein complex between putidaredoxin (Pdx) and cytochrome P450(cam) (CYP101) is the catalytically competent species for camphor hydroxylation by CYP101.	Camphor	129-136	calmodulin 3	Homo sapiens	56-76	
22468842-1	2012	Removal of substrate (+)-camphor from the active site of cytochrome P450(cam) (CYP101A1) results in nuclear magnetic resonance-detected perturbations in multiple regions of the enzyme.	Camphor	21-32	calmodulin 3	Homo sapiens	57-77	
22258082-2	2012	The determination of the reaction and activation volumes enabled the construction of the first complete volume profile for the reversible binding of camphor to P450(cam).	Camphor	149-156	calmodulin 3	Homo sapiens	160-169	
22258082-4	2012	Similarly, the activation volume determined for the dissociation of camphor is influenced by the presence of K(+), which reflects changes in the ease of water entering the active site of camphor-bound P450(cam) that depends on the K(+) concentration.	Camphor	68-75	calmodulin 3	Homo sapiens	201-210	
22258082-4	2012	Similarly, the activation volume determined for the dissociation of camphor is influenced by the presence of K(+), which reflects changes in the ease of water entering the active site of camphor-bound P450(cam) that depends on the K(+) concentration.	Camphor	187-194	calmodulin 3	Homo sapiens	201-210	
22258082-5	2012	Careful analysis of the components that contribute to the observed volume changes allowed the estimation of the total number of water molecules expelled to the bulk solvent during the binding of camphor to P450(cam) and the subsequent spin transition.	Camphor	195-202	calmodulin 3	Homo sapiens	206-215	
22258082-6	2012	The results are discussed in reference to other studies reported in the literature that deal with the kinetics and thermodynamics of the binding of camphor to P450(cam) under various reaction conditions.	Camphor	148-155	calmodulin 3	Homo sapiens	159-168	
22250969-3	2012	We investigated ET reactions between zinc-substituted cytochrome P450(cam) and small organic compounds such as quinones and ferrocene, which are capable of accessing the protein"s hydrophobic channel and binding close to the active site, like its native substrate, camphor.	Camphor	265-272	calmodulin 3	Homo sapiens	54-74	
21391540-1	2011	Vibrational coherence spectroscopy (VCS) is used to investigate the low-frequency dynamics of camphor-free and camphor-bound cytochrome P450(cam) (CYP 101) and its L358P mutant.	Camphor	111-118	calmodulin 3	Homo sapiens	125-145	
21391540-4	2011	The very low frequency region <=200 cm(-1), uniquely accessed by open-band VCS measurements, reveals a mode near 103 cm(-1) in P450(cam) when camphor is not present in the distal pocket.	Camphor	145-152	calmodulin 3	Homo sapiens	130-139	
16943206-1	2006	We have identified a P450(cam) mutation, L244A, that mitigates the affinity for imidazole and substituted imidazoles while maintaining a high affinity for the natural substrate camphor.	Camphor	177-184	calmodulin 3	Homo sapiens	21-30	
10587448-1	1999	Tris(2,2"-bipyridyl)ruthenium(II) was used as a light-induced artificial electron donor for the transfer of the first electron to cytochrome P-450(cam) bound with (1R)-camphor and camphane substrates, and in the substrate-free form.	Camphor	163-175	calmodulin 3	Homo sapiens	130-151