Correction: Franz et al. Unraveling a Force-Generating Allosteric Pathway of Actomyosin Communication Associated with ADP and Pi Release. Int. J. Mol. Sci. 2021, 22, 104.

The author wishes to make the following correction to this paper [...].

Table and Figure Legend

The author wishes to make the following correction to this paper [1]:

In the original article, there were following mistakes:

A common term was incorrectly used in the legend for Table 2. The incorrect parameters “Steady-state ATPase” should be replaced with “Steady-state ATPase Activity”. A parameter was incorrectly assigned in the legend for Table 4. The incorrect parameters “k′+5/K′5K′6” should be replaced with “k′+5K′5K′6”. Parameters were incorrectly assigned in the legend for Figure 5. The incorrect parameters “K′5K′6” should be replaced with “1/(K′5K′6)”. Parameters were incorrectly assigned in the legend for Figure 6. The incorrect parameters “K′DPAk+4” should be replaced with “k+4K′DPA”.

Error in Table

In the original article, there was a mistake in Table 3 as published. Rate and equilibrium constants, and corresponding values were incorrectly assigned. The corrected Table 3 appears below.

Table 3

Transient kinetic parameters and equilibrium constants in the absence of actin.

	Unit	M765wt	M765AA	M765GGG
ATP binding to myosin 1
K 1 k +2	(µM−1s−1)	0.48 ± 0.01	0.38 ± 0.01	0.38 ± 0.01
k −2	(s−1)	0.79 ± 0.49	0.54 ± 0.24	0.43 ± 0.25
k+3+k−3	(s−1)	42 ± 1	61 ± 2	106 ± 8
ADP binding to myosin 1
k −5 K 6	(µM−1s−1)	0.58 ± 0.02	0.38 ± 0.02	0.49 ± 0.01
k +5	(s−1)	1.6 ± 0.1	1.8 ± 0.1	1.9 ± 0.1
1/(K5K6)	(µM)	2.8 ± 0.2	4.7 ± 0.4	3.9 ± 0.2
Rate of Pi release 1
k +4	(s−1)	0.02 ± 0.01	n.d.	0.02 ± 0.01

1 at 20 °C.

In the original article, there were mistakes in Tables 4 and 5 as published. Rate and equilibrium constants and a unit were incorrectly assigned. The corrected Table 4 and Table 5 appear below.

Table 4

Transient kinetic parameters and equilibrium constants in the presence of actin.

	Unit	M765wt	M765AA	M765GGG
Actomyosin interactions in the absence and presence of ADP
k′ +A	(µM−1s−1)	0.64 ± 0.03	0.61 ± 0.03	0.61 ± 0.03
k′ -A	(s−1)	0.003	0.004	0.005
1/K′ A 1	(µM)	0.0057 ± 0.0005	0.010 ± 0.009	0.011 ± 0.009
k′ +DA	(µM−1s−1)	0.12 ± 0.01	n.d.	0.18 ± 0.01
k′ -DA	(s−1)	0.006 ± 0.001	n.d.	0.005 ± 0.001
1/K′ DA 2	(µM)	0.063 ± 0.002	n.d.	0.024 ± 0.001
ATP interactions of actomyosin
K′ 1 k′ +2	(µM−1s−1)	0.24 ± 0.01	0.32 ± 0.01	0.92 ± 0.01
k′ +2	(s−1)	719 ± 22	871 ± 80	923 ± 19
k′ −2	(s−1)	0.08 ± 0.05	0.62 ± 0.05	1.48 ± 0.13
1/K′ 1	(µM)	3200 ± 130	2702 ± 279	883 ± 30
ADP interactions of actomyosin
k′− 5 K′ 6 3	(µM−1s−1)	>1.0 / >0.74	>1.47 / >2.94	4.7 ± 1 / 3.6 ± 1 4
1/(K′5K′6)	(µM)	135 ± 10 5	34 ± 4 5	3.4 ± 1 6
k′+5	(s−1)	>100 7	>100 7	16 ± 1 8
Pi kinetics of actomyosin
k′ +4	(s−1)	3.8 ± 1.1	n.d.	14.4 ± 1.0
k′ +4 K′ DPA	(µM−1s−1)	0.04 ± 0.01	n.d.	0.79 ± 0.08
1/K′ DPA	(µM)	94 ± 32	n.d.	18 ± 3
Weak-to-strong transition
k′ weak-strong	(s−1)	1.0 ± 0.01	n.d.	2.6 ± 0.04
Duty ratio
tstrong/ttotal	%	3 ± 1	<4 ± 1	49 ± 4
Experimental	%	<1	n.d.	35

1 Calculated: /; 2 calculated: /; 3 calculated from ; 4 obtained from linear fit of kfast of competitive ATP/ADP binding experiment with 25 µM ATP; 5 obtained from ADP-inhibition of ATP-induced dissociation; 6 obtained from hyperbolic fits of Aslow and Afast (Figure 5g); 7 estimated form the rate of ADP inhibition of ATP-induced dissociation at excess ADP concentrations; 8 y-intercept of hyperbola in Figure 5i; n.d. not determined.

Table 5

Parameters used for the estimation of the fractional occupancies of intermediate states.

	Unit	M765 wt	M765 AA	M765 GGG
Equilibrium constants
K′ DPA	(µM−1)	0.01	0.01	0.05
K′ 4	(µM−1)	0.00001	0.00001	0.00001
K′ 5	-	0.5	0.74	7.14
K′ 6	(µM−1)	0.02	0.02	0.02
K′ 1	(µM−1)	0.0003	0.004	0.001
K′ 2	-	8988	1405	624
K′ TA	(µM−1)	0.001	0.001	0.001
K 3	-	9.5	9.2	9.6
K′ 3	-	95	92	96
Rate constants of forward reactions
k′ +DPA	(µM−1s−1)	10	10	50
k′ +4	(s−1)	3.8	5.0	14.4
k′ +5	(s−1)	235	160	20
k′ +6	(s−1)	1000	1000	1000
k′ +1	(µM−1s−1)	100	100	100
k′ +2	(s−1)	719	871	923
k′ +TA	(s−1)	1000	1000	1000
k +3	(s−1)	38	55	96
k′ +3	(s−1)	38	55	96
Rate constants of backwards reactions
k′ -DPA	(s−1)	1000	1000	1000
k′ −4	(µM−1s−1)	0.000038	0.00005	0.000144
k′ −5	(s−1)	470	216	2.8
k′ −6	(µM−1s−1)	20	20	20
k′ −1	(s−1)	333300	250000	88500
k′ −2	(s−1)	0.08	0.62	1.48
k′ -TA	(µM−1s−1)	1	1	1
k −3	(s−1)	4	6	10
k′ −3	(s−1)	0.4	0.6	1

Text Correction

There were following errors in the original article.

A correction has been made to 2. Results and Discussion:

Paragraph 8. The incorrect constants “K′5K′6” should be replaced with “1/(K′5K′6)”.

Paragraph 10. The incorrect constants “K′DPA” should be replaced with “1/K′DPA”. The incorrect constants “K′DPAk′+4” should be replaced with “k′+4K′DPA”.

Paragraph 11. The incorrect constants “K′DPA” should be replaced with “1/K′DPA”.

A correction has been made to 3. Conclusions, Paragraph 1. The incorrect constants “K′5K′6” should be replaced with “1/K′5K′6”.

The authors state that the scientific conclusions are unaffected. This correction was approved by the Academic Editor. The original publication has also been updated.